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* Residue conservation analysis
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PDB id:
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Complex (signal transduction/peptide)
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Title:
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Shc ptb domain complexed with a trka receptor phosphopeptide, nmr, minimized average structure
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Structure:
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Shc. Chain: a. Fragment: ptb domain. Engineered: yes. Trka receptor phosphopeptide. Chain: b. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Strain: bl21 (de3). Cell_line: bl21. Gene: ptb domain of shc. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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1 models
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Authors:
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M.-M.Zhou,K.S.Ravichandran,E.T.Olejniczak,A.M.Petros,R.P.Meadows, M.Sattler,J.E.Harlan,W.S.Wade,S.J.Burakoff,S.W.Fesik
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Key ref:
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M.M.Zhou
et al.
(1995).
Structure and ligand recognition of the phosphotyrosine binding domain of Shc.
Nature,
378,
584-592.
PubMed id:
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Date:
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27-Mar-96
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Release date:
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15-May-97
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PROCHECK
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Headers
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References
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Enzyme class:
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Chain B:
E.C.2.7.10.1
- receptor protein-tyrosine kinase.
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Reaction:
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
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L-tyrosyl-[protein]
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+
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ATP
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=
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O-phospho-L-tyrosyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Nature
378:584-592
(1995)
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PubMed id:
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Structure and ligand recognition of the phosphotyrosine binding domain of Shc.
|
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M.M.Zhou,
K.S.Ravichandran,
E.F.Olejniczak,
A.M.Petros,
R.P.Meadows,
M.Sattler,
J.E.Harlan,
W.S.Wade,
S.J.Burakoff,
S.W.Fesik.
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ABSTRACT
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The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB)
domain of Shc complexed to a phosphopeptide reveals an alternative means of
recognizing tyrosine-phosphorylated proteins. Unlike in SH2 domains, the
phosphopeptide forms an antiparallel beta-strand with a beta-sheet of the
protein, interacts with a hydrophobic pocket through the (pY-5) residue, and
adopts a beta-turn. The PTB domain is structurally similar to pleckstrin
homology domains (a beta-sandwich capped by an alpha-helix) and binds to acidic
phospholipids, suggesting a possible role in membrane localization.
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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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C.Chakraborty,
G.Agoramoorthy,
and
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(2011).
Exploring the evolutionary relationship of insulin receptor substrate family using computational biology.
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PLoS One,
6,
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B.Asbach,
M.Kolb,
M.Liss,
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and
M.Schäferling
(2010).
Protein microarray assay for the screening of SH3 domain interactions.
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| |
Anal Bioanal Chem,
398,
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The Lifespan-regulator p66Shc in mitochondria: redox enzyme or redox sensor?
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Antioxid Redox Signal,
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M.J.Smith,
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A.Starostine,
T.Pawson,
and
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(2010).
The PTB domain of ShcA couples receptor activation to the cytoskeletal regulator IQGAP1.
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| |
EMBO J,
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J.C.Grant,
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K.K.Jin,
H.E.Klock,
M.W.Knuth,
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A.Kumar,
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C.L.Rife,
N.Sefcovic,
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A.Godzik,
S.A.Lesley,
and
I.A.Wilson
(2010).
Bacterial pleckstrin homology domains: a prokaryotic origin for the PH domain.
|
| |
J Mol Biol,
396,
31-46.
|
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|
PDB codes:
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F.Finetti,
M.T.Savino,
and
C.T.Baldari
(2009).
Positive and negative regulation of antigen receptor signaling by the Shc family of protein adapters.
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| |
Immunol Rev,
232,
115-134.
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|
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S.M.Alam,
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L.Zhang,
and
M.F.Lin
(2009).
A novel role of Shc adaptor proteins in steroid hormone-regulated cancers.
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| |
Endocr Relat Cancer,
16,
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|
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S.S.Deepa,
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APPL1: role in adiponectin signaling and beyond.
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| |
Am J Physiol Endocrinol Metab,
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System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties.
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| |
Chem Biol,
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A.Kaushansky,
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(2008).
A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R.
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| |
Mol Biosyst,
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|
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E.Neumann-Haefelin,
W.Qi,
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SHC-1/p52Shc targets the insulin/IGF-1 and JNK signaling pathways to modulate life span and stress response in C. elegans.
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| |
Genes Dev,
22,
2721-2735.
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|
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|
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G.A.Kyriazis,
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Numb endocytic adapter proteins regulate the transport and processing of the amyloid precursor protein in an isoform-dependent manner: implications for Alzheimer disease pathogenesis.
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| |
J Biol Chem,
283,
25492-25502.
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|
|
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S.Ravaud,
S.Schlesinger,
J.Koch,
K.Beyreuther,
I.Sinning,
and
K.Wild
(2008).
Crystal structure of the human Fe65-PTB1 domain.
|
| |
J Biol Chem,
283,
23113-23120.
|
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|
PDB codes:
|
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|
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|
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K.Sakashita,
K.Mimori,
F.Tanaka,
Y.Kamohara,
H.Inoue,
T.Sawada,
K.Hirakawa,
and
M.Mori
(2008).
Prognostic relevance of Tensin4 expression in human gastric cancer.
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| |
Ann Surg Oncol,
15,
2606-2613.
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|
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|
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M.Leone,
E.C.Yu,
R.C.Liddington,
E.B.Pasquale,
and
M.Pellecchia
(2008).
The PTB domain of tensin: NMR solution structure and phosphoinositides binding studies.
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| |
Biopolymers,
89,
86-92.
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PDB code:
|
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P.A.Keyel,
J.R.Thieman,
R.Roth,
E.Erkan,
E.T.Everett,
S.C.Watkins,
J.E.Heuser,
and
L.M.Traub
(2008).
The AP-2 adaptor beta2 appendage scaffolds alternate cargo endocytosis.
|
| |
Mol Biol Cell,
19,
5309-5326.
|
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|
|
|
|
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W.Gong,
D.Zhou,
Y.Ren,
Y.Wang,
Z.Zuo,
Y.Shen,
F.Xiao,
Q.Zhu,
A.Hong,
X.Zhou,
X.Gao,
and
T.Li
(2008).
PepCyber:P~PEP: a database of human protein protein interactions mediated by phosphoprotein-binding domains.
|
| |
Nucleic Acids Res,
36,
D679-D683.
|
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|
|
|
|
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C.J.McCleverty,
D.C.Lin,
and
R.C.Liddington
(2007).
Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions.
|
| |
Protein Sci,
16,
1223-1229.
|
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|
PDB code:
|
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|
|
|
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|
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N.Jones,
W.R.Hardy,
M.B.Friese,
C.Jorgensen,
M.J.Smith,
N.M.Woody,
S.J.Burden,
and
T.Pawson
(2007).
Analysis of a Shc family adaptor protein, ShcD/Shc4, that associates with muscle-specific kinase.
|
| |
Mol Cell Biol,
27,
4759-4773.
|
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|
|
|
|
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Z.Ma,
D.P.Myers,
R.F.Wu,
F.E.Nwariaku,
and
L.S.Terada
(2007).
p66Shc mediates anoikis through RhoA.
|
| |
J Cell Biol,
179,
23-31.
|
 |
|
|
|
|
 |
H.Remaut,
and
G.Waksman
(2006).
Protein-protein interaction through beta-strand addition.
|
| |
Trends Biochem Sci,
31,
436-444.
|
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|
|
|
|
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M.J.Smith,
W.R.Hardy,
J.M.Murphy,
N.Jones,
and
T.Pawson
(2006).
Screening for PTB domain binding partners and ligand specificity using proteome-derived NPXY peptide arrays.
|
| |
Mol Cell Biol,
26,
8461-8474.
|
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|
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|
|
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P.Aloy,
and
R.B.Russell
(2006).
Structural systems biology: modelling protein interactions.
|
| |
Nat Rev Mol Cell Biol,
7,
188-197.
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|
|
|
|
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T.K.Lundgren,
R.P.Scott,
M.Smith,
T.Pawson,
and
P.Ernfors
(2006).
Engineering the recruitment of phosphotyrosine binding domain-containing adaptor proteins reveals distinct roles for RET receptor-mediated cell survival.
|
| |
J Biol Chem,
281,
29886-29896.
|
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|
|
|
|
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A.Lamberti,
O.Longo,
P.Del Vecchio,
N.Zambrano,
G.Barone,
T.Russo,
and
P.Arcari
(2005).
Probing the secondary structure of a recombinant neuronal adaptor protein and its phosphotyrosine binding domains.
|
| |
Biosci Biotechnol Biochem,
69,
2395-2400.
|
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|
|
|
|
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H.Sondermann,
and
J.Kuriyan
(2005).
C2 can do it, too.
|
| |
Cell,
121,
158-160.
|
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PDB code:
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K.N.Robinson,
K.Manto,
R.J.Buchsbaum,
J.I.MacDonald,
and
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(2005).
Neurotrophin-dependent tyrosine phosphorylation of Ras guanine-releasing factor 1 and associated neurite outgrowth is dependent on the HIKE domain of TrkA.
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| |
J Biol Chem,
280,
225-235.
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|
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|
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M.Nishi,
E.D.Werner,
B.C.Oh,
J.D.Frantz,
S.Dhe-Paganon,
L.Hansen,
J.Lee,
and
S.E.Shoelson
(2005).
Kinase activation through dimerization by human SH2-B.
|
| |
Mol Cell Biol,
25,
2607-2621.
|
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|
|
|
|
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P.C.Stolt,
Y.Chen,
P.Liu,
H.H.Bock,
S.C.Blacklow,
and
J.Herz
(2005).
Phosphoinositide binding by the disabled-1 PTB domain is necessary for membrane localization and Reelin signal transduction.
|
| |
J Biol Chem,
280,
9671-9677.
|
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|
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|
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R.Bauer,
B.Löer,
K.Ostrowski,
J.Martini,
A.Weimbs,
H.Lechner,
and
M.Hoch
(2005).
Intercellular communication: the Drosophila innexin multiprotein family of gap junction proteins.
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| |
Chem Biol,
12,
515-526.
|
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|
|
|
|
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W.Cho,
and
R.V.Stahelin
(2005).
Membrane-protein interactions in cell signaling and membrane trafficking.
|
| |
Annu Rev Biophys Biomol Struct,
34,
119-151.
|
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|
|
|
|
 |
A.Suenaga,
A.B.Kiyatkin,
M.Hatakeyama,
N.Futatsugi,
N.Okimoto,
Y.Hirano,
T.Narumi,
A.Kawai,
R.Susukita,
T.Koishi,
H.Furusawa,
K.Yasuoka,
N.Takada,
Y.Ohno,
M.Taiji,
T.Ebisuzaki,
J.B.Hoek,
A.Konagaya,
and
B.N.Kholodenko
(2004).
Tyr-317 phosphorylation increases Shc structural rigidity and reduces coupling of domain motions remote from the phosphorylation site as revealed by molecular dynamics simulations.
|
| |
J Biol Chem,
279,
4657-4662.
|
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PDB code:
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A.Ventura,
M.Maccarana,
V.A.Raker,
and
P.G.Pelicci
(2004).
A cryptic targeting signal induces isoform-specific localization of p46Shc to mitochondria.
|
| |
J Biol Chem,
279,
2299-2306.
|
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|
|
|
|
 |
H.Qin,
A.Percival-Smith,
C.Li,
C.Y.Jia,
G.Gloor,
and
S.S.Li
(2004).
A novel transmembrane protein recruits numb to the plasma membrane during asymmetric cell division.
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| |
J Biol Chem,
279,
11304-11312.
|
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|
|
|
|
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N.Shi,
S.Ye,
M.Bartlam,
M.Yang,
J.Wu,
Y.Liu,
F.Sun,
X.Han,
X.Peng,
B.Qiang,
J.Yuan,
and
Z.Rao
(2004).
Structural basis for the specific recognition of RET by the Dok1 phosphotyrosine binding domain.
|
| |
J Biol Chem,
279,
4962-4969.
|
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PDB codes:
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S.Pacini,
M.Pellegrini,
E.Migliaccio,
L.Patrussi,
C.Ulivieri,
A.Ventura,
F.Carraro,
A.Naldini,
L.Lanfrancone,
P.Pelicci,
and
C.T.Baldari
(2004).
p66SHC promotes apoptosis and antagonizes mitogenic signaling in T cells.
|
| |
Mol Cell Biol,
24,
1747-1757.
|
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|
|
|
|
 |
W.Cai,
J.Pei,
and
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(2004).
Reconstruction of ancestral protein sequences and its applications.
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| |
BMC Evol Biol,
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33.
|
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|
|
|
|
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A.Farooq,
L.Zeng,
K.S.Yan,
K.S.Ravichandran,
and
M.M.Zhou
(2003).
Coupling of folding and binding in the PTB domain of the signaling protein Shc.
|
| |
Structure,
11,
905-913.
|
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PDB codes:
|
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|
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|
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A.Q.Sun,
R.Salkar,
Sachchidanand,
S.Xu,
L.Zeng,
M.M.Zhou,
and
F.J.Suchy
(2003).
A 14-amino acid sequence with a beta-turn structure is required for apical membrane sorting of the rat ileal bile acid transporter.
|
| |
J Biol Chem,
278,
4000-4009.
|
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|
|
|
|
 |
K.S.Yan,
and
M.M.Zhou
(2003).
Examining both sides of a Janus PTB domain.
|
| |
Structure,
11,
482-484.
|
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|
|
|
|
 |
L.Zhang,
U.Lorenz,
and
K.S.Ravichandran
(2003).
Role of Shc in T-cell development and function.
|
| |
Immunol Rev,
191,
183-195.
|
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|
|
|
|
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M.Yun,
L.Keshvara,
C.G.Park,
Y.M.Zhang,
J.B.Dickerson,
J.Zheng,
C.O.Rock,
T.Curran,
and
H.W.Park
(2003).
Crystal structures of the Dab homology domains of mouse disabled 1 and 2.
|
| |
J Biol Chem,
278,
36572-36581.
|
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|
PDB codes:
|
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|
|
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|
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N.Schiering,
S.Knapp,
M.Marconi,
M.M.Flocco,
J.Cui,
R.Perego,
L.Rusconi,
and
C.Cristiani
(2003).
Crystal structure of the tyrosine kinase domain of the hepatocyte growth factor receptor c-Met and its complex with the microbial alkaloid K-252a.
|
| |
Proc Natl Acad Sci U S A,
100,
12654-12659.
|
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PDB codes:
|
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|
|
|
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|
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P.C.Stolt,
H.Jeon,
H.K.Song,
J.Herz,
M.J.Eck,
and
S.C.Blacklow
(2003).
Origins of peptide selectivity and phosphoinositide binding revealed by structures of disabled-1 PTB domain complexes.
|
| |
Structure,
11,
569-579.
|
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PDB codes:
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A.Faisal,
M.el-Shemerly,
D.Hess,
and
Y.Nagamine
(2002).
Serine/threonine phosphorylation of ShcA. Regulation of protein-tyrosine phosphatase-pest binding and involvement in insulin signaling.
|
| |
J Biol Chem,
277,
30144-30152.
|
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|
|
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|
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D.D.Chang,
B.Q.Hoang,
J.Liu,
and
T.A.Springer
(2002).
Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin.
|
| |
J Biol Chem,
277,
8140-8145.
|
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PDB code:
|
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|
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H.P.Su,
K.Nakada-Tsukui,
A.C.Tosello-Trampont,
Y.Li,
G.Bu,
P.M.Henson,
and
K.S.Ravichandran
(2002).
Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP).
|
| |
J Biol Chem,
277,
11772-11779.
|
 |
|
|
|
|
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K.S.Yan,
M.Kuti,
S.Yan,
S.Mujtaba,
A.Farooq,
M.P.Goldfarb,
and
M.M.Zhou
(2002).
FRS2 PTB domain conformation regulates interactions with divergent neurotrophic receptors.
|
| |
J Biol Chem,
277,
17088-17094.
|
 |
|
|
|
|
 |
K.Sato,
T.Nagao,
M.Kakumoto,
M.Kimoto,
T.Otsuki,
T.Iwasaki,
A.A.Tokmakov,
K.Owada,
and
Y.Fukami
(2002).
Adaptor protein Shc is an isoform-specific direct activator of the tyrosine kinase c-Src.
|
| |
J Biol Chem,
277,
29568-29576.
|
 |
|
|
|
|
 |
M.B.Yaffe
(2002).
Phosphotyrosine-binding domains in signal transduction.
|
| |
Nat Rev Mol Cell Biol,
3,
177-186.
|
 |
|
|
|
|
 |
S.R.Jaffrey,
F.Benfenati,
A.M.Snowman,
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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
codes are
shown on the right.
|
');
}
}
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