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* Residue conservation analysis
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PDB id:
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Signal transduction protein
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Title:
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Orientation of peptide fragments from sos proteins bound to the n- terminal sh3 domain of grb2 determined by nmr spectroscopy
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Structure:
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Growth factor receptor-bound protein 2. Chain: a. Engineered: yes. Sos-a peptide. Chain: b. Engineered: yes
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Source:
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Mus musculus. House mouse. Organism_taxid: 10090. Gene: mouse grb2. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Organism_taxid: 10090
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NMR struc:
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29 models
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Authors:
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M.Wittekind,C.Mapelli,B.T.Farmer,K.-L.Suen,V.Goldfarb,J.Tsao, T.Lavoie,M.Barbacid,C.A.Meyers,L.Mueller
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Key ref:
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M.Wittekind
et al.
(1994).
Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy.
Biochemistry,
33,
13531-13539.
PubMed id:
DOI:
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Date:
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12-Aug-94
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Release date:
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26-Jan-95
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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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Biochemistry
33:13531-13539
(1994)
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PubMed id:
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Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy.
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M.Wittekind,
C.Mapelli,
B.T.Farmer,
K.L.Suen,
V.Goldfarb,
J.Tsao,
T.Lavoie,
M.Barbacid,
C.A.Meyers,
L.Mueller.
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ABSTRACT
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NMR spectroscopy has been used to characterize the protein-protein interactions
between the mouse Grb2 (mGrb2) N-terminal SH3 domain complexed with a 15-residue
peptide (SPLLPKLPP-KTYKRE) corresponding to residues 1264-1278 of the mouse
Sos-2 (mSos-2) protein. Intermolecular interactions between the peptide and
13C-15N-labeled SH3 domain were identified in half-reverse-filtered 2D and 3D
NOESY experiments. Assignments for the protons involved in interactions between
the peptide and the SH3 domain were confirmed in a series of NOESY experiments
using a set of peptides in which different leucine positions were fully
deuterated. The peptide ligand-binding site of the mGrb2 N-terminal SH3 domain
is defined by the side chains of specific aromatic residues (Tyr7, Phe9, Trp36,
Tyr52) that form two hydrophobic subsites contacting the side chains of the
peptide Leu4 and Leu7 residues. An adjacent negatively charged subsite on the
SH3 surface is likely to interact with the side chain of a basic residue at
peptide position 10 that we show to be involved in binding. The peptide-binding
site of the SH3 is characterized by large perturbations of amide chemical shifts
when the peptide is added to the SH3 domain. The mGrb2 N-terminal SH3 domain
structure in the complex is well-defined (backbone RMSD of 0.56 +/- 0.21
calculated over the backbone N, C alpha, and C atoms of residues 1-54). The
structure of the peptide in the complex is less well-defined but displays a
distinct orientation.(ABSTRACT TRUNCATED AT 250 WORDS)
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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.Palencia,
A.Camara-Artigas,
M.T.Pisabarro,
J.C.Martinez,
and
I.Luque
(2010).
Role of interfacial water molecules in proline-rich ligand recognition by the Src homology 3 domain of Abl.
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J Biol Chem,
285,
2823-2833.
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PDB codes:
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C.B.McDonald,
K.L.Seldeen,
B.J.Deegan,
V.Bhat,
and
A.Farooq
(2010).
Assembly of the Sos1-Grb2-Gab1 ternary signaling complex is under allosteric control.
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Arch Biochem Biophys,
494,
216-225.
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S.Rauscher,
and
R.Pomès
(2010).
Molecular simulations of protein disorder.
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Biochem Cell Biol,
88,
269-290.
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C.B.McDonald,
K.L.Seldeen,
B.J.Deegan,
and
A.Farooq
(2009).
SH3 domains of Grb2 adaptor bind to PXpsiPXR motifs within the Sos1 nucleotide exchange factor in a discriminate manner.
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Biochemistry,
48,
4074-4085.
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S.Donnini,
and
A.H.Juffer
(2004).
Calculation of affinities of peptides for proteins.
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J Comput Chem,
25,
393-411.
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J.C.Ferreon,
and
V.J.Hilser
(2003).
The effect of the polyproline II (PPII) conformation on the denatured state entropy.
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Protein Sci,
12,
447-457.
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J.C.Ferreon,
and
V.J.Hilser
(2003).
Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling.
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Protein Sci,
12,
982-996.
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S.M.Feller,
G.Tuchscherer,
and
J.Voss
(2003).
High affinity molecules disrupting GRB2 protein complexes as a therapeutic strategy for chronic myelogenous leukaemia.
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Leuk Lymphoma,
44,
411-427.
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A.W.McGee,
S.R.Dakoji,
O.Olsen,
D.S.Bredt,
W.A.Lim,
and
K.E.Prehoda
(2001).
Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins.
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Mol Cell,
8,
1291-1301.
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PDB code:
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H.Korkaya,
S.Jameel,
D.Gupta,
S.Tyagi,
R.Kumar,
M.Zafrullah,
M.Mazumdar,
S.K.Lal,
L.Xiaofang,
D.Sehgal,
S.R.Das,
and
D.Sahal
(2001).
The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK.
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J Biol Chem,
276,
42389-42400.
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K.V.Kishan,
M.E.Newcomer,
T.H.Rhodes,
and
S.D.Guilliot
(2001).
Effect of pH and salt bridges on structural assembly: molecular structures of the monomer and intertwined dimer of the Eps8 SH3 domain.
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Protein Sci,
10,
1046-1055.
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PDB codes:
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N.Okishio,
M.Nagai,
R.Fukuda,
S.Nagatomo,
and
T.Kitagawa
(2000).
Interactions of phosphatidylinositol 3-kinase Src homology 3 domain with its ligand peptide studied by absorption, circular dichroism, and UV resonance raman spectroscopies.
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Biopolymers,
57,
208-217.
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N.Schiering,
E.Casale,
P.Caccia,
P.Giordano,
and
C.Battistini
(2000).
Dimer formation through domain swapping in the crystal structure of the Grb2-SH2-Ac-pYVNV complex.
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Biochemistry,
39,
13376-13382.
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PDB code:
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A.M.Mongioví,
P.R.Romano,
S.Panni,
M.Mendoza,
W.T.Wong,
A.Musacchio,
G.Cesareni,
and
P.P.Di Fiore
(1999).
A novel peptide-SH3 interaction.
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EMBO J,
18,
5300-5309.
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G.Wang,
G.P.Wylie,
P.D.Twigg,
D.L.Caspar,
J.R.Murphy,
and
T.M.Logan
(1999).
Solution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor protein.
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Proc Natl Acad Sci U S A,
96,
6119-6124.
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PDB code:
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L.Buday
(1999).
Membrane-targeting of signalling molecules by SH2/SH3 domain-containing adaptor proteins.
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Biochim Biophys Acta,
1422,
187-204.
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T.Ago,
H.Nunoi,
T.Ito,
and
H.Sumimoto
(1999).
Mechanism for phosphorylation-induced activation of the phagocyte NADPH oxidase protein p47(phox). Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47(phox), thereby activating the oxidase.
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J Biol Chem,
274,
33644-33653.
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M.Vidal,
J.L.Montiel,
D.Cussac,
F.Cornille,
M.Duchesne,
F.Parker,
B.Tocqué,
B.P.Roques,
and
C.Garbay
(1998).
Differential interactions of the growth factor receptor-bound protein 2 N-SH3 domain with son of sevenless and dynamin. Potential role in the Ras-dependent signaling pathway.
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J Biol Chem,
273,
5343-5348.
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R.K.Rasmussen,
H.Ji,
J.S.Eddes,
R.L.Moritz,
G.E.Reid,
R.J.Simpson,
and
D.S.Dorow
(1998).
Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins.
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Electrophoresis,
19,
809-817.
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S.Knapp,
P.T.Mattson,
P.Christova,
K.D.Berndt,
A.Karshikoff,
M.Vihinen,
C.I.Smith,
and
R.Ladenstein
(1998).
Thermal unfolding of small proteins with SH3 domain folding pattern.
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Proteins,
31,
309-319.
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D.C.Dalgarno,
M.C.Botfield,
and
R.J.Rickles
(1997).
SH3 domains and drug design: ligands, structure, and biological function.
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Biopolymers,
43,
383-400.
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J.R.Engen,
T.E.Smithgall,
W.H.Gmeiner,
and
D.L.Smith
(1997).
Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry.
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Biochemistry,
36,
14384-14391.
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N.A.Farrow,
O.Zhang,
J.D.Forman-Kay,
and
L.E.Kay
(1997).
Characterization of the backbone dynamics of folded and denatured states of an SH3 domain.
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Biochemistry,
36,
2390-2402.
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O.Zhang,
and
J.D.Forman-Kay
(1997).
NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
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Biochemistry,
36,
3959-3970.
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D.A.Renzoni,
D.J.Pugh,
G.Siligardi,
P.Das,
C.J.Morton,
C.Rossi,
M.D.Waterfield,
I.D.Campbell,
and
J.E.Ladbury
(1996).
Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.
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Biochemistry,
35,
15646-15653.
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PDB codes:
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E.C.Petrella,
L.M.Machesky,
D.A.Kaiser,
and
T.D.Pollard
(1996).
Structural requirements and thermodynamics of the interaction of proline peptides with profilin.
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Biochemistry,
35,
16535-16543.
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M.T.Pisabarro,
and
L.Serrano
(1996).
Rational design of specific high-affinity peptide ligands for the Abl-SH3 domain.
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Biochemistry,
35,
10634-10640.
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W.A.Lim
(1996).
Reading between the lines: SH3 recognition of an intact protein.
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Structure,
4,
657-659.
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A.M.Gronenborn,
and
G.M.Clore
(1995).
Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy.
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Crit Rev Biochem Mol Biol,
30,
351-385.
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B.J.Mayer,
and
M.J.Eck
(1995).
SH3 domains. Minding your p's and q's.
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Curr Biol,
5,
364-367.
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C.H.Lee,
B.Leung,
M.A.Lemmon,
J.Zheng,
D.Cowburn,
J.Kuriyan,
and
K.Saksela
(1995).
A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein.
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EMBO J,
14,
5006-5015.
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J.A.Simon,
and
S.L.Schreiber
(1995).
Grb2 SH3 binding to peptides from Sos: evaluation of a general model for SH3-ligand interactions.
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Chem Biol,
2,
53-60.
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T.Raabe,
J.P.Olivier,
B.Dickson,
X.Liu,
G.D.Gish,
T.Pawson,
and
E.Hafen
(1995).
Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.
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EMBO J,
14,
2509-2518.
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Y.Q.Gosser,
J.Zheng,
M.Overduin,
B.J.Mayer,
and
D.Cowburn
(1995).
The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
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Structure,
3,
1075-1086.
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PDB code:
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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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