1i4t: Difference between revisions

Revision as of 10:25, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1i4t.png

Template:STRUCTURE 1i4t

CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN COMPLEX WITH ARFAPTINCRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN COMPLEX WITH ARFAPTIN

Template:ABSTRACT PUBMED 11346801

About this StructureAbout this Structure

1I4T is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways., Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ, Nature. 2001 May 10;411(6834):215-9. PMID:11346801

Page seeded by OCA on Tue Jul 1 10:25:07 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1i4t.gif|left|200px]]
+{{Seed}}
+[[Image:1i4t.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1i4t|  PDB=1i4t  |  SCENE=  }}
-'''CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN COMPLEX WITH ARFAPTIN'''
+===CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN COMPLEX WITH ARFAPTIN===
-==Overview==
+<!--
-Small G proteins are GTP-dependent molecular switches that regulate numerous cellular functions. They can be classified into homologous subfamilies that are broadly associated with specific biological processes. Cross-talk between small G-protein families has an important role in signalling, but the mechanism by which it occurs is poorly understood. The coordinated action of Arf and Rho family GTPases is required to regulate many cellular processes including lipid signalling, cell motility and Golgi function. Arfaptin is a ubiquitously expressed protein implicated in mediating cross-talk between Rac (a member of the Rho family) and Arf small GTPases. Here we show that Arfaptin binds specifically to GTP-bound Arf1 and Arf6, but binds to Rac.GTP and Rac.GDP with similar affinities. The X-ray structure of Arfaptin reveals an elongated, crescent-shaped dimer of three-helix coiled-coils. Structures of Arfaptin with Rac bound to either GDP or the slowly hydrolysable analogue GMPPNP show that the switch regions adopt similar conformations in both complexes. Our data highlight fundamental differences between the molecular mechanisms of Rho and Ras family signalling, and suggest a model of Arfaptin-mediated synergy between the Arf and Rho family signalling pathways.
+The line below this paragraph, {{ABSTRACT_PUBMED_11346801}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11346801 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11346801}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: G-protein]]
 [[Category: Signaling protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:34:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:25:07 2008''