1k40
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(New page: 200px<br /><applet load="1k40" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k40, resolution 2.25Å" /> '''crystal structure of...)
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Revision as of 16:43, 20 November 2007
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crystal structure of the FAT domain of focal adhesion kinase
Overview
Focal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling complexes that are formed following engagement of, the extracellular matrix by integrins. The C-terminal 'focal adhesion, targeting' (FAT) region is necessary and sufficient for localizing FAK to, focal adhesions. We have determined the crystal structure of FAT and show, that it forms a four-helix bundle that resembles those found in two other, proteins involved in cell adhesion, alpha-catenin and vinculin. The, binding of FAT to the focal adhesion protein, paxillin, requires the, integrity of the helical bundle, whereas binding to another focal adhesion, protein, talin, does not. We show by mutagenesis that paxillin binding, involves two hydrophobic patches on opposite faces of the bundle and, propose a model in which two LD motifs of paxillin adopt amphipathic, helices that augment the hydrophobic core of FAT, creating a six-helix, bundle.
About this Structure
1K40 is a Single protein structure of sequence from Mus musculus. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin., Hayashi I, Vuori K, Liddington RC, Nat Struct Biol. 2002 Feb;9(2):101-6. PMID:11799401
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