1k05

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{{STRUCTURE_1k05| PDB=1k05 | SCENE= }}
{{STRUCTURE_1k05| PDB=1k05 | SCENE= }}
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'''Crystal structure of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase'''
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===Crystal structure of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase===
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==Overview==
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The localization of focal adhesion kinase (FAK) to sites of integrin clustering initiates downstream signaling. The C-terminal focal adhesion targeting (FAT) domain causes this localization by interacting with talin and paxillin. FAT also mediates signaling through Grb2 via phosphorylated Y925. We report two crystal structures of the FAT domain. Large rearrangements of the structure are indicated to allow phosphorylation of Y925 and subsequent interaction with Grb2. Sequence homology and structural compatibility suggest a FAT-like fold for the C-terminal domains of CAS, Efs/Sin, and HEF1. A structure-based alignment including these proteins and the vinculin tail domain reveals a conserved region that could play a role in focal adhesion targeting. Previously postulated "paxillin binding subdomains" may contribute to structural integrity rather than directly to paxillin binding.
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(as it appears on PubMed at http://www.pubmed.gov), where 12005431 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12005431}}
==About this Structure==
==About this Structure==
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[[Category: Noble, M E.M.]]
[[Category: Noble, M E.M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:08:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:27:31 2008''

Revision as of 20:27, 27 July 2008

Image:1k05.png

Template:STRUCTURE 1k05

Crystal structure of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase

Template:ABSTRACT PUBMED 12005431

About this Structure

1K05 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structural basis of localization and signaling by the focal adhesion targeting domain., Arold ST, Hoellerer MK, Noble ME, Structure. 2002 Mar;10(3):319-27. PMID:12005431

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