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PDBsum entry 2dwv
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Protein binding
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PDB id
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2dwv
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Protein binding
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Title:
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Solution structure of the second ww domain from mouse salvador homolog 1 protein (mww45)
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Structure:
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Salvador homolog 1 protein. Chain: a, b. Fragment: the second ww domain. Synonym: 45 kda ww domain protein, mww45. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Gene: sav1, ww45, wwp3. Other_details: cell-free protein synthesis
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NMR struc:
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20 models
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Authors:
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S.Ohnishi,T.Kigawa,S.Koshiba,T.Tomizawa,M.Sato,N.Tochio,M.Inoue, T.Harada,S.Watanabe,P.Guntert,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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S.Ohnishi
et al.
(2007).
Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form.
Febs Lett,
581,
462-468.
PubMed id:
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Date:
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17-Aug-06
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Release date:
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17-Feb-07
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PROCHECK
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Headers
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References
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Q8VEB2
(SAV1_MOUSE) -
Protein salvador homolog 1 from Mus musculus
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Seq:
Struc:
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386 a.a.
49 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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*
PDB and UniProt seqs differ
at 10 residue positions (black
crosses)
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Febs Lett
581:462-468
(2007)
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PubMed id:
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Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form.
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S.Ohnishi,
P.Güntert,
S.Koshiba,
T.Tomizawa,
R.Akasaka,
N.Tochio,
M.Sato,
M.Inoue,
T.Harada,
S.Watanabe,
A.Tanaka,
M.Shirouzu,
T.Kigawa,
S.Yokoyama.
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ABSTRACT
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The WW domain is known as one of the smallest protein modules with a
triple-stranded beta-sheet fold. Here, we present the solution structure of the
second WW domain from the mouse salvador homolog 1 protein. This WW domain forms
a homodimer with a beta-clam-like motif, as evidenced by size exclusion
chromatography, analytical ultracentrifugation and NMR spectroscopy. While
typical WW domains are believed to function as monomeric modules that recognize
proline-rich sequences, by using conserved aromatic and hydrophobic residues
that are solvent-exposed on the surface of the beta-sheet, this WW domain buries
these residues in the dimer interface.
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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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S.W.Chan,
C.J.Lim,
L.Chen,
Y.F.Chong,
C.Huang,
H.Song,
and
W.Hong
(2011).
The Hippo pathway in biological control and cancer development.
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J Cell Physiol,
226,
928-939.
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H.Oh,
and
K.D.Irvine
(2010).
Yorkie: the final destination of Hippo signaling.
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Trends Cell Biol,
20,
410-417.
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J.Yu,
Y.Zheng,
J.Dong,
S.Klusza,
W.M.Deng,
and
D.Pan
(2010).
Kibra functions as a tumor suppressor protein that regulates Hippo signaling in conjunction with Merlin and Expanded.
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Dev Cell,
18,
288-299.
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L.Chen,
P.G.Loh,
and
H.Song
(2010).
Structural and functional insights into the TEAD-YAP complex in the Hippo signaling pathway.
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Protein Cell,
1,
1073-1083.
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M.Sudol,
and
K.F.Harvey
(2010).
Modularity in the Hippo signaling pathway.
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Trends Biochem Sci,
35,
627-633.
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R.Senturia,
M.Faller,
S.Yin,
J.A.Loo,
D.Cascio,
M.R.Sawaya,
D.Hwang,
R.T.Clubb,
and
F.Guo
(2010).
Structure of the dimerization domain of DiGeorge critical region 8.
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Protein Sci,
19,
1354-1365.
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PDB code:
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S.Ohnishi,
N.Tochio,
T.Tomizawa,
R.Akasaka,
T.Harada,
E.Seki,
M.Sato,
S.Watanabe,
Y.Fujikura,
S.Koshiba,
T.Terada,
M.Shirouzu,
A.Tanaka,
T.Kigawa,
and
S.Yokoyama
(2008).
Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily.
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Protein Sci,
17,
1531-1541.
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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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Links
