1gcq: Difference between revisions
New page: left|200px<br /> <applet load="1gcq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gcq, resolution 1.68Å" /> '''CRYSTAL STRUCTURE O... |
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'''CRYSTAL STRUCTURE OF VAV AND GRB2 SH3 DOMAINS'''<br /> | '''CRYSTAL STRUCTURE OF VAV AND GRB2 SH3 DOMAINS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1GCQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MRD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1GCQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: vav]] | [[Category: vav]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:52:34 2008'' | ||
Revision as of 16:52, 15 February 2008
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CRYSTAL STRUCTURE OF VAV AND GRB2 SH3 DOMAINS
OverviewOverview
Vav is a guanine nucleotide exchange factor for the Rho/Rac family that is, expressed exclusively in hematopoietic cells. Growth factor receptor-bound, protein 2 (Grb2) has been proposed to play important roles in the membrane, localization and activation of Vav through dimerization of its C-terminal, Src-homology 3 (SH3) domain (GrbS) and the N-terminal SH3 domain of Vav, (VavS). The crystal structure of VavS complexed with GrbS has been solved., VavS is distinct from other SH3 domain proteins in that its binding site, for proline-rich peptides is blocked by its own RT loop. One of the ends, of the VavS beta-barrel forms a concave hydrophobic surface. The GrbS, components make a contiguous complementary interface with the VavS, surface. The binding site of GrbS for VavS partially overlaps with the, canonical binding site for proline-rich peptides, but is definitely, different. Mutations at the interface caused a decrease in the binding, affinity of VavS for GrbS by 4- to 40-fold. The structure reveals how GrbS, discriminates VavS specifically from other signaling molecules without, binding to the proline-rich motif.
DiseaseDisease
Known diseases associated with this structure: Central hypoventilation syndrome, congenital OMIM:[100790], Haddad syndrome OMIM:[100790]
About this StructureAbout this Structure
1GCQ is a Protein complex structure of sequences from Homo sapiens and Mus musculus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Novel recognition mode between Vav and Grb2 SH3 domains., Nishida M, Nagata K, Hachimori Y, Horiuchi M, Ogura K, Mandiyan V, Schlessinger J, Inagaki F, EMBO J. 2001 Jun 15;20(12):2995-3007. PMID:11406576
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