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PDBsum entry 1a5r
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Targeting protein
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PDB id
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1a5r
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Contents |
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* Residue conservation analysis
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PDB id:
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Targeting protein
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Title:
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Structure determination of the small ubiquitin-related modifier sumo- 1, nmr, 10 structures
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Structure:
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Sumo-1. Chain: a. Synonym: pic1, gmp1, ubl1, sentrin. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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NMR struc:
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10 models
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Authors:
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P.Bayer,A.Arndt,S.Metzger,R.Mahajan,F.Melchior,R.Jaenicke,J.Becker
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Key ref:
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P.Bayer
et al.
(1998).
Structure determination of the small ubiquitin-related modifier SUMO-1.
J Mol Biol,
280,
275-286.
PubMed id:
DOI:
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Date:
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18-Feb-98
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Release date:
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14-Oct-98
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PROCHECK
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Headers
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References
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P63165
(SUMO1_HUMAN) -
Small ubiquitin-related modifier 1 from Homo sapiens
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Seq:
Struc:
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101 a.a.
103 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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J Mol Biol
280:275-286
(1998)
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PubMed id:
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Structure determination of the small ubiquitin-related modifier SUMO-1.
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P.Bayer,
A.Arndt,
S.Metzger,
R.Mahajan,
F.Melchior,
R.Jaenicke,
J.Becker.
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ABSTRACT
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The recently discovered small ubiquitin-related modifier SUMO-1 belongs to the
growing family of ubiquitin-related proteins involved in postranslational
protein modification. Unlike ubiquitin, SUMO-1 does not appear to target
proteins for degradation but seems to be involved in the modulation of
protein-protein interactions. Independent studies demonstrate an essential
function of SUMO-1 in the regulation of nucleo-cytoplasmic transport, and
suggest a role in cell-cycle regulation and apoptosis. Here, we present the
first three-dimensional structure of SUMO-1 solved by NMR. Although having only
18% amino acid sequence identity with ubiquitin, the overall structure closely
resembles that of ubiquitin, featuring the betabetaalphabetabetaalphabeta fold
of the ubiquitin protein family. In addition, the position of the two C-terminal
Gly residues required for isopeptide bond formation is conserved between
ubiquitin and SUMO-1. The most prominent feature of SUMO-1 is a long and highly
flexible N terminus, which protrudes from the core of the protein and which is
absent in ubiquitin. Furthermore, ubiquitin Lys48, required to generate
ubiquitin polymers, is substituted in SUMO-1 by Gln69 at the same position,
which provides an explanation of why SUMO-1 has not been observed to form
polymers. Moreover, the hydrophobic core of SUMO-1 and ubiquitin is maintained
by conserved hydrophobic residues, whereas the overall charge topology of SUMO-1
and ubiquitin differs significantly, suggesting specific modifying enzymes and
target proteins for both proteins.
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Selected figure(s)
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Figure 6.
Figure 6. Stereo view of a superposition of the structures
of SUMO-1 (black) and ubiquitin (red) using the Program O [Jones
et al 1991]. The overlay of the C^α backbone shows the
similarity between the two protein cores of SUMO-1 and
ubiquitin, although these proteins share only 18% sequence
identity. Also marked are side-chains of Gln69 of SUMO-1 and
Lys48 of ubiquitin, which is important for the formation of
polyubiquitin and which are located at the same position. The
indicated C-terminal di-glycine motif is localized in a very
flexible region, functionally conserved and located in similar
positions relative to the overall protein fold.
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Figure 7.
Figure 7. Comparison of the surfaces of SUMO-1 (a and b)
and ubiquitin (c and d). Shown are two opposite surface views of
SUMO-1 and ubiquitin rotated around the longitudinal axis by
160° and by ±80° as compared to the front view
shown in Figure 5 and Figure 6. The corresponding orientations
are indicated by the C^α backbone visible underneath the
surface. The charge topology was calculated and coloured
according to the electrostatic potential over a range of
approximately −20 kT/e (in red) to +20 kT/e (in blue) using
the program GRASP [Nicholls et al 1991]. The first view of
SUMO-1 (a) displays positive charged epitopes (Arg54, Lys46,
Lys25, Lys23, Lys17 and Lys16) absent on the corresponding
surface of ubiquitin (c) with the exception of SUMO-1 Lys25 (a),
and ubiquitin Lys6 (c). The second view of SUMO-1 (b) reveals a
large negatively charged surface (Glu89, Asp86, Glu85 and Glu84)
together with a negatively charged pocket (Glu83, Glu18, Glu15,
Asp12, Glu11 and Glu20), which are not conserved on the
corresponding surface of ubiquitin (d).
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1998,
280,
275-286)
copyright 1998.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Barry,
and
R.B.Lock
(2011).
Small ubiquitin-related modifier-1: Wrestling with protein regulation.
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Int J Biochem Cell Biol,
43,
37-40.
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B.Cox,
J.Briscoe,
and
F.Ulloa
(2010).
SUMOylation by Pias1 regulates the activity of the Hedgehog dependent Gli transcription factors.
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PLoS One,
5,
e11996.
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C.T.Archer,
and
T.Kodadek
(2010).
The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases.
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Nucleic Acids Res,
38,
789-796.
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J.M.Reed,
C.Dervinis,
A.M.Morse,
and
J.M.Davis
(2010).
The SUMO conjugation pathway in Populus: genomic analysis, tissue-specific and inducible SUMOylation and in vitro de-SUMOylation.
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Planta,
232,
51-59.
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K.Saito,
W.Kagawa,
T.Suzuki,
H.Suzuki,
S.Yokoyama,
H.Saitoh,
S.Tashiro,
N.Dohmae,
and
H.Kurumizaka
(2010).
The putative nuclear localization signal of the human RAD52 protein is a potential sumoylation site.
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J Biochem,
147,
833-842.
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P.Cao,
J.Yu,
W.Lu,
X.Cai,
Z.Wang,
Z.Gu,
J.Zhang,
T.Ye,
and
M.Wang
(2010).
Expression and purification of an antitumor-analgesic peptide from the venom of Mesobuthus martensii Karsch by small ubiquitin-related modifier fusion in Escherichia coli.
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Biotechnol Prog,
26,
1240-1244.
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A.Korb,
H.Pavenstädt,
and
T.Pap
(2009).
Cell death in rheumatoid arthritis.
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Apoptosis,
14,
447-454.
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A.Skilton,
J.C.Ho,
B.Mercer,
E.Outwin,
and
F.Z.Watts
(2009).
SUMO chain formation is required for response to replication arrest in S. pombe.
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PLoS One,
4,
e6750.
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B.Lee,
and
M.T.Muller
(2009).
SUMOylation enhances DNA methyltransferase 1 activity.
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Biochem J,
421,
449-461.
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D.Kumar,
J.Chugh,
S.Sharma,
and
R.V.Hosur
(2009).
Conserved structural and dynamics features in the denatured states of drosophila SUMO, human SUMO and ubiquitin proteins: Implications to sequence-folding paradigm.
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Proteins,
76,
387-402.
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T.Jadhav,
and
M.W.Wooten
(2009).
Defining an Embedded Code for Protein Ubiquitination.
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J Proteomics Bioinform,
2,
316.
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Z.Xu,
H.Y.Chan,
W.L.Lam,
K.H.Lam,
L.S.Lam,
T.B.Ng,
and
S.W.Au
(2009).
SUMO proteases: redox regulation and biological consequences.
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Antioxid Redox Signal,
11,
1453-1484.
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C.Y.Wang,
and
J.X.She
(2008).
SUMO4 and its role in type 1 diabetes pathogenesis.
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Diabetes Metab Res Rev,
24,
93.
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H.Li,
L.Gao,
Z.Shen,
C.Y.Li,
K.Li,
M.Li,
Y.J.Lv,
C.X.Li,
T.W.Gao,
and
Y.F.Liu
(2008).
Association study of NFKB1 and SUMO4 polymorphisms in Chinese patients with psoriasis vulgaris.
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Arch Dermatol Res,
300,
425-433.
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J.J.Perry,
J.A.Tainer,
and
M.N.Boddy
(2008).
A SIM-ultaneous role for SUMO and ubiquitin.
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Trends Biochem Sci,
33,
201-208.
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L.A.Campbell,
E.J.Faivre,
M.D.Show,
J.G.Ingraham,
J.Flinders,
J.D.Gross,
and
H.A.Ingraham
(2008).
Decreased recognition of SUMO-sensitive target genes following modification of SF-1 (NR5A1).
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Mol Cell Biol,
28,
7476-7486.
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N.Issar,
E.Roux,
D.Mattei,
and
A.Scherf
(2008).
Identification of a novel post-translational modification in Plasmodium falciparum: protein sumoylation in different cellular compartments.
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Cell Microbiol,
10,
1999-2011.
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P.L.Andersen,
F.Xu,
and
W.Xiao
(2008).
Eukaryotic DNA damage tolerance and translesion synthesis through covalent modifications of PCNA.
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Cell Res,
18,
162-173.
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Y.Wang,
I.Ladunga,
A.R.Miller,
K.M.Horken,
T.Plucinak,
D.P.Weeks,
and
C.P.Bailey
(2008).
The small ubiquitin-like modifier (SUMO) and SUMO-conjugating system of Chlamydomonas reinhardtii.
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Genetics,
179,
177-192.
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Z.Sun,
Z.Xia,
F.Bi,
and
J.N.Liu
(2008).
Expression and purification of human urodilatin by small ubiquitin-related modifier fusion in Escherichia coli.
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Appl Microbiol Biotechnol,
78,
495-502.
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Z.Tang,
C.M.Hecker,
A.Scheschonka,
and
H.Betz
(2008).
Protein interactions in the sumoylation cascade: lessons from X-ray structures.
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FEBS J,
275,
3003-3015.
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D.M.Duda,
R.C.van Waardenburg,
L.A.Borg,
S.McGarity,
A.Nourse,
M.B.Waddell,
M.A.Bjornsti,
and
B.A.Schulman
(2007).
Structure of a SUMO-binding-motif mimic bound to Smt3p-Ubc9p: conservation of a non-covalent ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway.
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J Mol Biol,
369,
619-630.
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PDB code:
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R.Chosed,
D.R.Tomchick,
C.A.Brautigam,
S.Mukherjee,
V.S.Negi,
M.Machius,
and
K.Orth
(2007).
Structural analysis of Xanthomonas XopD provides insights into substrate specificity of ubiquitin-like protein proteases.
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J Biol Chem,
282,
6773-6782.
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PDB codes:
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R.Geiss-Friedlander,
and
F.Melchior
(2007).
Concepts in sumoylation: a decade on.
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Nat Rev Mol Cell Biol,
8,
947-956.
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S.Martin,
K.A.Wilkinson,
A.Nishimune,
and
J.M.Henley
(2007).
Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction.
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Nat Rev Neurosci,
8,
948-959.
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X.H.Mascle,
D.Germain-Desprez,
P.Huynh,
P.Estephan,
and
M.Aubry
(2007).
Sumoylation of the transcriptional intermediary factor 1beta (TIF1beta), the Co-repressor of the KRAB Multifinger proteins, is required for its transcriptional activity and is modulated by the KRAB domain.
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J Biol Chem,
282,
10190-10202.
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X.Yuan,
Y.Kuramitsu,
H.Furumoto,
X.Zhang,
E.Hayashi,
M.Fujimoto,
and
K.Nakamura
(2007).
Nuclear protein profiling of Jurkat cells during heat stress-induced apoptosis by 2-DE and MS/MS.
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Electrophoresis,
28,
2018-2026.
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Y.K.Lee,
S.N.Thomas,
A.J.Yang,
and
D.K.Ann
(2007).
Doxorubicin down-regulates Kruppel-associated box domain-associated protein 1 sumoylation that relieves its transcription repression on p21WAF1/CIP1 in breast cancer MCF-7 cells.
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J Biol Chem,
282,
1595-1606.
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Z.Deng,
M.Wan,
and
G.Sui
(2007).
PIASy-mediated sumoylation of Yin Yang 1 depends on their interaction but not the RING finger.
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Mol Cell Biol,
27,
3780-3792.
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A.Kumar,
S.Srivastava,
R.K.Mishra,
R.Mittal,
and
R.V.Hosur
(2006).
Local structural preferences and dynamics restrictions in the urea-denatured state of SUMO-1: NMR characterization.
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Biophys J,
90,
2498-2509.
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B.P.Downes,
S.A.Saracco,
S.S.Lee,
D.N.Crowell,
and
R.D.Vierstra
(2006).
MUBs, a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation.
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J Biol Chem,
281,
27145-27157.
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C.M.Hecker,
M.Rabiller,
K.Haglund,
P.Bayer,
and
I.Dikic
(2006).
Specification of SUMO1- and SUMO2-interacting motifs.
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J Biol Chem,
281,
16117-16127.
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J.G.Marblestone,
S.C.Edavettal,
Y.Lim,
P.Lim,
X.Zuo,
and
T.R.Butt
(2006).
Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO.
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Protein Sci,
15,
182-189.
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J.Xu,
J.Zhang,
L.Wang,
J.Zhou,
H.Huang,
J.Wu,
Y.Zhong,
and
Y.Shi
(2006).
Solution structure of Urm1 and its implications for the origin of protein modifiers.
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Proc Natl Acad Sci U S A,
103,
11625-11630.
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PDB code:
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M.S.Macauley,
W.J.Errington,
M.Schärpf,
C.D.Mackereth,
A.G.Blaszczak,
B.J.Graves,
and
L.P.McIntosh
(2006).
Beads-on-a-string, characterization of ETS-1 sumoylated within its flexible N-terminal sequence.
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J Biol Chem,
281,
4164-4172.
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Z.Wang,
G.M.Jones,
and
G.Prelich
(2006).
Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in Saccharomyces cerevisiae.
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Genetics,
172,
1499-1509.
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D.Baba,
N.Maita,
J.G.Jee,
Y.Uchimura,
H.Saitoh,
K.Sugasawa,
F.Hanaoka,
H.Tochio,
H.Hiroaki,
and
M.Shirakawa
(2005).
Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.
|
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Nature,
435,
979-982.
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PDB code:
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H.Ding,
Y.Yang,
J.Zhang,
J.Wu,
H.Liu,
and
Y.Shi
(2005).
Structural basis for SUMO-E2 interaction revealed by a complex model using docking approach in combination with NMR data.
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Proteins,
61,
1050-1058.
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PDB code:
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J.M.Desterro,
L.P.Keegan,
E.Jaffray,
R.T.Hay,
M.A.O'Connell,
and
M.Carmo-Fonseca
(2005).
SUMO-1 modification alters ADAR1 editing activity.
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Mol Biol Cell,
16,
5115-5126.
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J.Narasimhan,
M.Wang,
Z.Fu,
J.M.Klein,
A.L.Haas,
and
J.J.Kim
(2005).
Crystal structure of the interferon-induced ubiquitin-like protein ISG15.
|
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J Biol Chem,
280,
27356-27365.
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PDB code:
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J.Song,
Z.Zhang,
W.Hu,
and
Y.Chen
(2005).
Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation.
|
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J Biol Chem,
280,
40122-40129.
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PDB code:
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L.M.Lois,
and
C.D.Lima
(2005).
Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1.
|
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EMBO J,
24,
439-451.
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PDB codes:
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M.Novatchkova,
A.Bachmair,
B.Eisenhaber,
and
F.Eisenhaber
(2005).
Proteins with two SUMO-like domains in chromatin-associated complexes: the RENi (Rad60-Esc2-NIP45) family.
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BMC Bioinformatics,
6,
22.
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Y.G.Gao,
A.X.Song,
Y.H.Shi,
Y.G.Chang,
S.X.Liu,
Y.Z.Yu,
X.T.Cao,
D.H.Lin,
and
H.Y.Hu
(2005).
Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells.
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Protein Sci,
14,
2044-2050.
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PDB code:
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A.C.Vertegaal,
S.C.Ogg,
E.Jaffray,
M.S.Rodriguez,
R.T.Hay,
J.S.Andersen,
M.Mann,
and
A.I.Lamond
(2004).
A proteomic study of SUMO-2 target proteins.
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J Biol Chem,
279,
33791-33798.
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D.Reverter,
and
C.D.Lima
(2004).
A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex.
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Structure,
12,
1519-1531.
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PDB codes:
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E.S.Johnson
(2004).
Protein modification by SUMO.
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Annu Rev Biochem,
73,
355-382.
|
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J.Hemelaar,
A.Borodovsky,
B.M.Kessler,
D.Reverter,
J.Cook,
N.Kolli,
T.Gan-Erdene,
K.D.Wilkinson,
G.Gill,
C.D.Lima,
H.L.Ploegh,
and
H.Ovaa
(2004).
Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins.
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Mol Cell Biol,
24,
84-95.
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J.Song,
L.K.Durrin,
T.A.Wilkinson,
T.G.Krontiris,
and
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(2004).
Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.
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Proc Natl Acad Sci U S A,
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M.Novatchkova,
R.Budhiraja,
G.Coupland,
F.Eisenhaber,
and
A.Bachmair
(2004).
SUMO conjugation in plants.
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Planta,
220,
1-8.
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M.S.Macauley,
W.J.Errington,
M.Okon,
M.Schärpf,
C.D.Mackereth,
B.A.Schulman,
and
L.P.McIntosh
(2004).
Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1.
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J Biol Chem,
279,
49131-49137.
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P.Dieckhoff,
M.Bolte,
Y.Sancak,
G.H.Braus,
and
S.Irniger
(2004).
Smt3/SUMO and Ubc9 are required for efficient APC/C-mediated proteolysis in budding yeast.
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| |
Mol Microbiol,
51,
1375-1387.
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R.K.Mishra,
S.S.Jatiani,
A.Kumar,
V.R.Simhadri,
R.V.Hosur,
and
R.Mittal
(2004).
Dynamin interacts with members of the sumoylation machinery.
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J Biol Chem,
279,
31445-31454.
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W.C.Huang,
T.P.Ko,
S.S.Li,
and
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(2004).
Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins.
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| |
Eur J Biochem,
271,
4114-4122.
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|
PDB codes:
|
|
|
|
|
|
|
|
E.M.Eaton,
and
L.Sealy
(2003).
Modification of CCAAT/enhancer-binding protein-beta by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3.
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J Biol Chem,
278,
33416-33421.
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G.Gill
(2003).
Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity.
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Curr Opin Genet Dev,
13,
108-113.
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H.Walden,
M.S.Podgorski,
D.T.Huang,
D.W.Miller,
R.J.Howard,
D.L.Minor,
J.M.Holton,
and
B.A.Schulman
(2003).
The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1.
|
| |
Mol Cell,
12,
1427-1437.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
J.Kurepa,
J.M.Walker,
J.Smalle,
M.M.Gosink,
S.J.Davis,
T.L.Durham,
D.Y.Sung,
and
R.D.Vierstra
(2003).
The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress.
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J Biol Chem,
278,
6862-6872.
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J.Lüders,
G.Pyrowolakis,
and
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(2003).
The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP.
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EMBO Rep,
4,
1169-1174.
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J.S.Seeler,
and
A.Dejean
(2003).
Nuclear and unclear functions of SUMO.
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Nat Rev Mol Cell Biol,
4,
690-699.
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M.J.Rudolph,
M.M.Wuebbens,
O.Turque,
K.V.Rajagopalan,
and
H.Schindelin
(2003).
Structural studies of molybdopterin synthase provide insights into its catalytic mechanism.
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J Biol Chem,
278,
14514-14522.
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|
PDB codes:
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|
|
|
|
|
|
|
S.Holmstrom,
M.E.Van Antwerp,
and
J.A.Iñiguez-Lluhi
(2003).
Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy.
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| |
Proc Natl Acad Sci U S A,
100,
15758-15763.
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S.J.Li,
and
M.Hochstrasser
(2003).
The Ulp1 SUMO isopeptidase: distinct domains required for viability, nuclear envelope localization, and substrate specificity.
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| |
J Cell Biol,
160,
1069-1081.
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T.D.Mueller,
and
J.Feigon
(2003).
Structural determinants for the binding of ubiquitin-like domains to the proteasome.
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EMBO J,
22,
4634-4645.
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|
PDB codes:
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|
|
|
|
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|
|
T.McNally,
Q.Huang,
R.S.Janis,
Z.Liu,
E.T.Olejniczak,
and
R.M.Reilly
(2003).
Structural analysis of UBL5, a novel ubiquitin-like modifier.
|
| |
Protein Sci,
12,
1562-1566.
|
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|
PDB code:
|
|
|
|
|
|
|
|
W.J.Hung,
R.S.Roberson,
J.Taft,
and
D.Y.Wu
(2003).
Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions.
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| |
Mol Cell Biol,
23,
3477-3486.
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C.Villalva,
P.Trempat,
C.Greenland,
C.Thomas,
J.P.Girard,
F.Moebius,
G.Delsol,
and
P.Brousset
(2002).
Isolation of differentially expressed genes in NPM-ALK-positive anaplastic large cell lymphoma.
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| |
Br J Haematol,
118,
791-798.
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K.I.Kim,
S.H.Baek,
and
C.H.Chung
(2002).
Versatile protein tag, SUMO: its enzymology and biological function.
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| |
J Cell Physiol,
191,
257-268.
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K.J.Walters,
M.F.Kleijnen,
A.M.Goh,
G.Wagner,
and
P.M.Howley
(2002).
Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a.
|
| |
Biochemistry,
41,
1767-1777.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
K.Uchiyama,
E.Jokitalo,
F.Kano,
M.Murata,
X.Zhang,
B.Canas,
R.Newman,
C.Rabouille,
D.Pappin,
P.Freemont,
and
H.Kondo
(2002).
VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo.
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| |
J Cell Biol,
159,
855-866.
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M.L.Spengler,
K.Kurapatwinski,
A.R.Black,
and
J.Azizkhan-Clifford
(2002).
SUMO-1 modification of human cytomegalovirus IE1/IE72.
|
| |
J Virol,
76,
2990-2996.
|
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N.Kotaja,
U.Karvonen,
O.A.Jänne,
and
J.J.Palvimo
(2002).
PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases.
|
| |
Mol Cell Biol,
22,
5222-5234.
|
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|
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|
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W.Sheng,
and
X.Liao
(2002).
Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions.
|
| |
Protein Sci,
11,
1482-1491.
|
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|
PDB code:
|
|
|
|
|
|
|
|
E.Mossessova,
and
C.D.Lima
(2000).
Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.
|
| |
Mol Cell,
5,
865-876.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
F.Melchior
(2000).
SUMO--nonclassical ubiquitin.
|
| |
Annu Rev Cell Dev Biol,
16,
591-626.
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N.D.Kurniawan,
A.R.Atkins,
S.Bieri,
C.J.Brown,
I.M.Brereton,
P.A.Kroon,
and
R.Smith
(2000).
NMR structure of a concatemer of the first and second ligand-binding modules of the human low-density lipoprotein receptor.
|
| |
Protein Sci,
9,
1282-1293.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
S.J.Li,
and
M.Hochstrasser
(2000).
The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein.
|
| |
Mol Cell Biol,
20,
2367-2377.
|
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Y.Mao,
M.Sun,
S.D.Desai,
and
L.F.Liu
(2000).
SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage.
|
| |
Proc Natl Acad Sci U S A,
97,
4046-4051.
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A.M.Wyndham,
R.T.Baker,
and
G.Chelvanayagam
(1999).
The Ubp6 family of deubiquitinating enzymes contains a ubiquitin-like domain: SUb.
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| |
Protein Sci,
8,
1268-1275.
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C.Kretz-Remy,
and
R.M.Tanguay
(1999).
SUMO/sentrin: protein modifiers regulating important cellular functions.
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| |
Biochem Cell Biol,
77,
299-309.
|
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|
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|
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C.S.Brower,
A.Shilatifard,
T.Mather,
T.Kamura,
Y.Takagi,
D.Haque,
A.Treharne,
S.I.Foundling,
J.W.Conaway,
and
R.C.Conaway
(1999).
The elongin B ubiquitin homology domain. Identification of Elongin B sequences important for interaction with Elongin C.
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| |
J Biol Chem,
274,
13629-13636.
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K.Tanaka,
J.Nishide,
K.Okazaki,
H.Kato,
O.Niwa,
T.Nakagawa,
H.Matsuda,
M.Kawamukai,
and
Y.Murakami
(1999).
Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation.
|
| |
Mol Cell Biol,
19,
8660-8672.
|
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Q.Liu,
C.Jin,
X.Liao,
Z.Shen,
D.J.Chen,
and
Y.Chen
(1999).
The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1).
|
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J Biol Chem,
274,
16979-16987.
|
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R.C.Hillig,
L.Renault,
I.R.Vetter,
T.Drell,
A.Wittinghofer,
and
J.Becker
(1999).
The crystal structure of rna1p: a new fold for a GTPase-activating protein.
|
| |
Mol Cell,
3,
781-791.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
T.Sternsdorf,
K.Jensen,
B.Reich,
and
H.Will
(1999).
The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers.
|
| |
J Biol Chem,
274,
12555-12566.
|
|
|
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|
C.Rao-Naik,
W.delaCruz,
J.M.Laplaza,
S.Tan,
J.Callis,
and
A.J.Fisher
(1998).
The rub family of ubiquitin-like proteins. Crystal structure of Arabidopsis rub1 and expression of multiple rubs in Arabidopsis.
|
| |
J Biol Chem,
273,
34976-34982.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
F.G.Whitby,
G.Xia,
C.M.Pickart,
and
C.P.Hill
(1998).
Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes.
|
| |
J Biol Chem,
273,
34983-34991.
|
|
|
PDB code:
|
|
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|
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|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
|
|
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