2j0m: Difference between revisions

Revision as of 15:52, 27 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:2j0m.png

Template:STRUCTURE 2j0m

CRYSTAL STRUCTURE A TWO-CHAIN COMPLEX BETWEEN THE FERM AND KINASE DOMAINS OF FOCAL ADHESION KINASE.CRYSTAL STRUCTURE A TWO-CHAIN COMPLEX BETWEEN THE FERM AND KINASE DOMAINS OF FOCAL ADHESION KINASE.

Template:ABSTRACT PUBMED 17574028

About this StructureAbout this Structure

2J0M is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the autoinhibition of focal adhesion kinase., Lietha D, Cai X, Ceccarelli DF, Li Y, Schaller MD, Eck MJ, Cell. 2007 Jun 15;129(6):1177-87. PMID:17574028

Page seeded by OCA on Sun Jul 27 15:52:54 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2j0m.jpg|left|200px]]
+{{Seed}}
+[[Image:2j0m.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2j0m|  PDB=2j0m  |  SCENE=  }}
-'''CRYSTAL STRUCTURE A TWO-CHAIN COMPLEX BETWEEN THE FERM AND KINASE DOMAINS OF FOCAL ADHESION KINASE.'''
+===CRYSTAL STRUCTURE A TWO-CHAIN COMPLEX BETWEEN THE FERM AND KINASE DOMAINS OF FOCAL ADHESION KINASE.===
-==Overview==
+<!--
-Appropriate tyrosine kinase signaling depends on coordinated sequential coupling of protein-protein interactions with catalytic activation. Focal adhesion kinase (FAK) integrates signals from integrin and growth factor receptors to regulate cellular responses including cell adhesion, migration, and survival. Here, we describe crystal structures representing both autoinhibited and active states of FAK. The inactive structure reveals a mechanism of inhibition in which the N-terminal FERM domain directly binds the kinase domain, blocking access to the catalytic cleft and protecting the FAK activation loop from Src phosphorylation. Additionally, the FERM domain sequesters the Tyr397 autophosphorylation and Src recruitment site, which lies in the linker connecting the FERM and kinase domains. The active phosphorylated FAK kinase adopts a conformation that is immune to FERM inhibition. Our biochemical and structural analysis shows how the architecture of autoinhibited FAK orchestrates an activation sequence of FERM domain displacement, linker autophosphorylation, Src recruitment, and full catalytic activation.
+The line below this paragraph, {{ABSTRACT_PUBMED_17574028}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17574028 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17574028}}
 ==About this Structure==
@@ Line 38: / Line 42: @@
 [[Category: Transferase]]
 [[Category: Tyrosine-protein kinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:10:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:52:54 2008''