1gcp: Difference between revisions

Revision as of 13:48, 21 February 2008

CRYSTAL STRUCTURE OF VAV SH3 DOMAIN

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.

About this StructureAbout this Structure

1GCP is a Single protein structure of sequence from Mus musculus. 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

Page seeded by OCA on Thu Feb 21 12:48:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1gcp.jpg|left|200px]]<br /><applet load="1gcp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1gcp.jpg|left|200px]]<br /><applet load="1gcp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1gcp, resolution 2.1&Aring;" />
 '''CRYSTAL STRUCTURE OF VAV SH3 DOMAIN'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-GCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GCP OCA].
+GCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCP OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: vav]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:56:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:42 2008''