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Contents |
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340 a.a.
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68 a.a.
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217 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Complex (transducer/transduction)
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Title:
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Phosducin/transducin beta-gamma complex
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Structure:
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Transducin. Chain: b. Fragment: lys-c resistant fragment, the gamma subunit cleaved after residue 68. Synonym: gt beta-gamma. Transducin. Chain: g. Fragment: lys-c resistant fragment, the gamma subunit cleaved after residue 68.
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Source:
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Bos taurus. Cattle. Organism_taxid: 9913. Cell_line: b834. Organ: eye. Tissue: retina. Cellular_location: rod outer segments. Other_details: purified from bovine rod outer segments. Rattus norvegicus.
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Biol. unit:
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Trimer (from
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Resolution:
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2.40Å
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R-factor:
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0.190
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R-free:
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0.277
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Authors:
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R.Gaudet,A.Bohm,P.B.Sigler
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Key ref:
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R.Gaudet
et al.
(1996).
Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin.
Cell,
87,
577-588.
PubMed id:
DOI:
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Date:
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06-Jan-97
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Release date:
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05-Jun-97
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PROCHECK
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Headers
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References
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P62871
(GBB1_BOVIN) -
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 from Bos taurus
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Seq:
Struc:
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340 a.a.
340 a.a.*
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DOI no:
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Cell
87:577-588
(1996)
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PubMed id:
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Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin.
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R.Gaudet,
A.Bohm,
P.B.Sigler.
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ABSTRACT
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The crystal structure of transducin's betagamma subunits complexed with
phosducin, which regulates Gtbetagamma activity, has been solved to 2.4
angstroms resolution. Phosducin has two domains that wrap around Gtbetagamma to
form an extensive interface. The N-terminal domain binds loops on the "top"
Gtbeta surface, overlapping the Gtalpha binding surface, explaining how
phosducin blocks Gtbetagamma's interaction with Gtalpha. The C-terminal domain
shows structural homology to thioredoxin and binds the outer strands of Gtbeta's
seventh and first blades in a manner likely to disrupt Gtbetagamma's normal
orientation relative to the membrane and receptor. Phosducin's Ser-73, which
when phosphorylated inhibits phosducin's function, points away from Gtbetagamma,
toward a large flexible loop. Thus phosphorylation is not likely to affect the
interface directly, but rather indirectly through an induced conformational
change.
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Selected figure(s)
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Figure 4.
Figure 4. Structure of Phosducin(A) Stereo pair showing the
Cα trace of phosducin in the complex. The trace for residues 37
to 66 (open bars) is tentative. The N-terminal domain is at the
top and the C-terminal domain is at the bottom of the figure.
G[t]βγ would be located to the right of the N-terminal domain.
The Ser-73 α carbon is enlarged and labeled. This figure was
generated by DPLOT (G. Van Duyne).(B) Stereo pair showing the
least-squares superimposed Cα traces of the phosducin
C-terminal domain (blue) and thioredoxin ([18]) (red). The N-
and C-terminal residues of the C-terminal domain are labeled
P111 and P230, respectively. The N- and C-terminus of
thioredoxin are labeled T1 and T108. The C-terminal domain is
viewed from its left side, relative to (A), in an orientation
similar to that in Figure 6A.
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Figure 8.
Figure 8. Electrostatic Potential Representation of
Phosducin/G[t]βγ and G[t]βγ AloneElectrostatic potential
contoured at +1.5 kT (blue) and −1.5 kT (red) (ionic STRENGTH
= 100 mM). On the left is the phosducin/G[t]βγ complex, in the
same orientation as in Figure 6A. On the right is G[t]βγ
alone, in the same orientation. This figure was generated using
GRASP ([33]).
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1996,
87,
577-588)
copyright 1996.
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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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C.Xu,
and
J.Min
(2011).
Structure and function of WD40 domain proteins.
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Protein Cell,
2,
202-214.
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PDB codes:
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F.W.Schmitges,
A.B.Prusty,
M.Faty,
A.Stützer,
G.M.Lingaraju,
J.Aiwazian,
R.Sack,
D.Hess,
L.Li,
S.Zhou,
R.D.Bunker,
U.Wirth,
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A.Bauer,
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J.Gu,
H.Gut,
W.Fischle,
J.Müller,
and
N.H.Thomä
(2011).
Histone Methylation by PRC2 Is Inhibited by Active Chromatin Marks.
|
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Mol Cell,
42,
330-341.
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PDB codes:
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|
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N.Beetz,
and
L.Hein
(2011).
The physiological roles of phosducin: from retinal function to stress-dependent hypertension.
|
| |
Cell Mol Life Sci,
68,
599-612.
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M.S.Park,
N.K.Itoga,
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B.M.Willardson,
and
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(2010).
NMR analysis of G-protein betagamma subunit complexes reveals a dynamic G(alpha)-Gbetagamma subunit interface and multiple protein recognition modes.
|
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Proc Natl Acad Sci U S A,
107,
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C.U.Stirnimann,
E.Petsalaki,
R.B.Russell,
and
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WD40 proteins propel cellular networks.
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Trends Biochem Sci,
35,
565-574.
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and
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(2010).
Visualization of the interaction between Gbetagamma and tubulin during light-induced cell elongation of Blepharisma japonicum.
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Photochem Photobiol Sci,
9,
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S.J.Ludtke,
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and
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(2010).
Structure of an apoptosome-procaspase-9 CARD complex.
|
| |
Structure,
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PDB codes:
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A.C.Howlett,
A.J.Gray,
J.M.Hunter,
and
B.M.Willardson
(2009).
Role of Molecular Chaperones in G Protein {beta}5/Regulator of G Protein Signaling Dimer Assembly and G Protein {beta}{gamma} Dimer Specificity.
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J Biol Chem,
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Prediction of protein-protein interfaces on G-protein beta subunits reveals a novel phospholipase C beta2 binding domain.
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392,
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J.S.Gutkind,
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(2009).
Differential Inhibitor of G{beta}{gamma} Signaling to AKT and ERK Derived from Phosducin-like Protein: EFFECT ON SPHINGOSINE 1-PHOSPHATE-INDUCED ENDOTHELIAL CELL MIGRATION AND IN VITRO ANGIOGENESIS.
|
| |
J Biol Chem,
284,
18334-18346.
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|
|
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M.D.Harrison,
M.Brede,
X.Zong,
M.J.Urbanski,
A.Sietmann,
J.Kaufling,
M.Barrot,
M.W.Seeliger,
M.A.Vieira-Coelho,
P.Hamet,
D.Gaudet,
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J.Tremblay,
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M.Kaldunski,
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and
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(2009).
Phosducin influences sympathetic activity and prevents stress-induced hypertension in humans and mice.
|
| |
J Clin Invest,
119,
3597-3612.
|
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|
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X.Lou,
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C.Z.Zhou,
and
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(2009).
Structure of the thioredoxin-fold domain of human phosducin-like protein 2.
|
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
67-70.
|
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PDB code:
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|
|
|
|
|
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A.García-Regalado,
M.L.Guzmán-Hernández,
I.Ramírez-Rangel,
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J.Vázquez-Prado,
and
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(2008).
G protein-coupled receptor-promoted trafficking of Gbeta1gamma2 leads to AKT activation at endosomes via a mechanism mediated by Gbeta1gamma2-Rab11a interaction.
|
| |
Mol Biol Cell,
19,
4188-4200.
|
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|
|
A.V.Smrcka
(2008).
G protein betagamma subunits: central mediators of G protein-coupled receptor signaling.
|
| |
Cell Mol Life Sci,
65,
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A.V.Smrcka,
D.M.Lehmann,
and
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(2008).
G protein betagamma subunits as targets for small molecule therapeutic development.
|
| |
Comb Chem High Throughput Screen,
11,
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C.A.Johnston,
A.J.Kimple,
P.M.Giguère,
and
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(2008).
Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2.
|
| |
Structure,
16,
1086-1094.
|
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PDB code:
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|
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M.Kosloff,
E.Alexov,
V.Y.Arshavsky,
and
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(2008).
Electrostatic and Lipid Anchor Contributions to the Interaction of Transducin with Membranes: MECHANISTIC IMPLICATIONS FOR ACTIVATION AND TRANSLOCATION.
|
| |
J Biol Chem,
283,
31197-31207.
|
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|
|
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J.T.Snyder,
S.Gershburg,
D.P.Siderovski,
T.K.Harden,
and
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(2008).
Crystal structure of the multifunctional Gbeta5-RGS9 complex.
|
| |
Nat Struct Mol Biol,
15,
155-162.
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PDB code:
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M.Schmoll
(2008).
The information highways of a biotechnological workhorse--signal transduction in Hypocrea jecorina.
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| |
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(2008).
Light-dependent compartmentalization of transducin in rod photoreceptors.
|
| |
Mol Neurobiol,
37,
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and
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(2008).
Dopamine modulates diurnal and circadian rhythms of protein phosphorylation in photoreceptor cells of mouse retina.
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27,
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M.S.Lee,
S.E.Tsutakawa,
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J.A.Tainer,
and
J.N.Glover
(2008).
The BARD1 C-terminal domain structure and interactions with polyadenylation factor CstF-50.
|
| |
Biochemistry,
47,
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and
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(2008).
Distinct Roles for Two G{alpha} G Interfaces in Cell Polarity Control by a Yeast Heterotrimeric G Protein.
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Mol Biol Cell,
19,
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and
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(2008).
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| |
Curr Pharm Biotechnol,
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B.M.Willardson,
and
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(2007).
Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding.
|
| |
Cell Signal,
19,
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|
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|
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M.Sokolov,
Y.M.Chen,
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R.Herrmann,
V.Y.Arshavsky,
and
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(2007).
Phosducin regulates the expression of transducin betagamma subunits in rod photoreceptors and does not contribute to phototransduction adaptation.
|
| |
J Gen Physiol,
130,
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|
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|
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|
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H.Song,
M.Belcastro,
E.J.Young,
and
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(2007).
Compartment-specific phosphorylation of phosducin in rods underlies adaptation to various levels of illumination.
|
| |
J Biol Chem,
282,
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|
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J.B.Blumer,
A.V.Smrcka,
and
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(2007).
Mechanistic pathways and biological roles for receptor-independent activators of G-protein signaling.
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| |
Pharmacol Ther,
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M.Srayko,
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A.A.Hyman,
and
M.R.Leroux
(2007).
Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression.
|
| |
Mol Biol Cell,
18,
2336-2345.
|
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Z.Han,
X.Xing,
M.Hu,
Y.Zhang,
P.Liu,
and
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(2007).
Structural basis of EZH2 recognition by EED.
|
| |
Structure,
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PDB code:
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B.H.Jennings,
L.M.Pickles,
S.M.Wainwright,
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and
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(2006).
Molecular recognition of transcriptional repressor motifs by the WD domain of the Groucho/TLE corepressor.
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| |
Mol Cell,
22,
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PDB codes:
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C.Klenk,
J.Humrich,
U.Quitterer,
and
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(2006).
SUMO-1 controls the protein stability and the biological function of phosducin.
|
| |
J Biol Chem,
281,
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C.M.Baker,
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T.Hu,
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(2006).
Mechanism of assembly of G protein betagamma subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex.
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| |
J Biol Chem,
281,
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V.Simon,
and
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(2006).
Accessory proteins for G proteins: partners in signaling.
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| |
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PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates.
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| |
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and
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and
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(2006).
Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5.
|
| |
Mol Cell,
22,
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PDB codes:
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G.L.Lukov,
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| |
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J Mol Biol,
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|
| |
Mol Cell Biol,
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C.Bermel,
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(2005).
Phosducin-like protein regulates G-protein betagamma folding by interaction with tailless complex polypeptide-1alpha: dephosphorylation or splicing of PhLP turns the switch toward regulation of Gbetagamma folding.
|
| |
J Biol Chem,
280,
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(2005).
Identification of residues in the WD-40 repeat motif of the F-box protein Met30p required for interaction with its substrate Met4p.
|
| |
Mol Genet Genomics,
273,
361-370.
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M.E.Burns,
and
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(2005).
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|
| |
Neuron,
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and
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(2005).
G protein betagamma directly regulates SNARE protein fusion machinery for secretory granule exocytosis.
|
| |
Nat Neurosci,
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|
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Ytm1, Nop7, and Erb1 form a complex necessary for maturation of yeast 66S preribosomes.
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Selection of gbeta subunits with point mutations that fail to activate specific signaling pathways in vivo: dissecting cellular responses mediated by a heterotrimeric G protein in Dictyostelium discoideum.
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Mol Biol Cell,
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Structural aspects of heterotrimeric G-protein signaling.
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A small region in phosducin inhibits G-protein betagamma-subunit function.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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only a partial list as not all journals are covered by
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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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