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164 a.a.
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(+ 1 more)
172 a.a.
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* Residue conservation analysis
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PDB id:
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Signaling protein
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Title:
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Crystal structure of the histone domain of son of sevenless
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Structure:
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Son of sevenless protein. Chain: a, b, c, d, e, f, g, h, i. Fragment: n-terminal histone domain. Synonym: sos-1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: sos1. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Nonamer (from
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Resolution:
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3.21Å
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R-factor:
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0.255
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R-free:
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0.292
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Authors:
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H.Sondermann,S.M.Soisson,D.Bar-Sagi,J.Kuriyan
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Key ref:
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H.Sondermann
et al.
(2003).
Tandem histone folds in the structure of the N-terminal segment of the ras activator Son of Sevenless.
Structure,
11,
1583-1593.
PubMed id:
DOI:
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Date:
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24-Aug-03
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Release date:
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09-Dec-03
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PROCHECK
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Headers
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References
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DOI no:
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Structure
11:1583-1593
(2003)
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PubMed id:
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Tandem histone folds in the structure of the N-terminal segment of the ras activator Son of Sevenless.
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H.Sondermann,
S.M.Soisson,
D.Bar-Sagi,
J.Kuriyan.
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ABSTRACT
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The Ras activator Son of Sevenless (Sos) contains a Cdc25 homology domain,
responsible for nucleotide exchange, as well as Dbl/Pleckstrin homology (DH/PH)
domains. We have determined the crystal structure of the N-terminal segment of
human Sos1 (residues 1-191) and show that it contains two tandem histone folds.
While the N-terminal domain is monomeric in solution, its structure is
surprisingly similar to that of histone dimers, with both subunits of the
histone "dimer" being part of the same peptide chain. One histone fold
corresponds to the region of Sos that is clearly similar in sequence to histones
(residues 91-191), whereas the other is formed by residues in Sos (1-90) that
are unrelated in sequence to histones. Residues that form a contiguous patch on
the surface of the histone domain of Sos are conserved from C. elegans to
humans, suggesting a potential role for this domain in protein-protein
interactions.
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Selected figure(s)
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Figure 4.
Figure 4. Comparison of the Histone Domain of Sos with the
Structures of Various Histone ProteinsSuperpositions were
generated by TOP3D (Lu, 2000). The histone domain of Sos is
shown in gray. The darker gray represents the C-terminal H2A
homology region. Rms deviations for the Ca backbone atoms
between structures being compared are indicated. Alignment with
the nucleosomal core histone dimers H2A/H2B (A) and H3/H4 (B)
are shown. H2A is colored in light green, H2B in dark green. H3
and H4 are shown in orange and red, respectively (PDB code:
1KX5; Davey et al., 2002). (C) Alignment with Methanopyrus
kandleri histone (PDB code: 1F1E; Fahrner et al., 2001).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
1583-1593)
copyright 2003.
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Figure was
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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A.Fernández-Medarde,
and
E.Santos
(2011).
The RasGrf family of mammalian guanine nucleotide exchange factors.
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Biochim Biophys Acta,
1815,
170-188.
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K.K.Yadav,
and
D.Bar-Sagi
(2010).
Allosteric gating of Son of sevenless activity by the histone domain.
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Proc Natl Acad Sci U S A,
107,
3436-3440.
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M.Tumurkhuu,
M.Saitoh,
A.Sato,
K.Takahashi,
M.Mimaki,
J.Takita,
K.Takeshita,
T.Hama,
A.Oka,
and
M.Mizuguchi
(2010).
Comprehensive genetic analysis of overlapping syndromes of RAS/RAF/MEK/ERK pathway.
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Pediatr Int,
52,
557-562.
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P.Walker,
D.Doenecke,
and
J.Kahle
(2009).
Importin 13 Mediates Nuclear Import of Histone Fold-containing Chromatin Accessibility Complex Heterodimers.
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J Biol Chem,
284,
11652-11662.
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J.Gureasko,
W.J.Galush,
S.Boykevisch,
H.Sondermann,
D.Bar-Sagi,
J.T.Groves,
and
J.Kuriyan
(2008).
Membrane-dependent signal integration by the Ras activator Son of sevenless.
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Nat Struct Mol Biol,
15,
452-461.
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A.E.Roberts,
T.Araki,
K.D.Swanson,
K.T.Montgomery,
T.A.Schiripo,
V.A.Joshi,
L.Li,
Y.Yassin,
A.M.Tamburino,
B.G.Neel,
and
R.S.Kucherlapati
(2007).
Germline gain-of-function mutations in SOS1 cause Noonan syndrome.
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Nat Genet,
39,
70-74.
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L.Mariño-Ramírez,
B.Hsu,
A.D.Baxevanis,
and
D.Landsman
(2006).
The Histone Database: a comprehensive resource for histones and histone fold-containing proteins.
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Proteins,
62,
838-842.
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N.Zarich,
J.L.Oliva,
N.Martínez,
R.Jorge,
A.Ballester,
S.Gutiérrez-Eisman,
S.García-Vargas,
and
J.M.Rojas
(2006).
Grb2 is a negative modulator of the intrinsic Ras-GEF activity of hSos1.
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Mol Biol Cell,
17,
3591-3597.
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C.Greco,
E.Sacco,
M.Vanoni,
and
L.De Gioia
(2005).
Identification and in silico analysis of a new group of double-histone fold-containing proteins.
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J Mol Model,
12,
76-84.
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C.Greco,
P.Fantucci,
and
L.De Gioia
(2005).
In silico functional characterization of a double histone fold domain from the Heliothis zea virus 1.
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BMC Bioinformatics,
6,
S15.
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H.Sondermann,
S.M.Soisson,
S.Boykevisch,
S.S.Yang,
D.Bar-Sagi,
and
J.Kuriyan
(2004).
Structural analysis of autoinhibition in the Ras activator Son of sevenless.
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Cell,
119,
393-405.
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PDB codes:
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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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Links
