2h7e
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(New page: 200px<br /><applet load="2h7e" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h7e" /> '''Solution structure of the talin F3 domain in...)
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Revision as of 09:27, 21 November 2007
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Solution structure of the talin F3 domain in complex with a chimeric beta3 integrin-PIP kinase peptide- minimized average structure
Overview
Regulation of integrin affinity (activation) is essential for metazoan, development and for many pathological processes. Binding of the talin, phosphotyrosine-binding (PTB) domain to integrin beta subunit cytoplasmic, domains (tails) causes activation, whereas numerous other, PTB-domain-containing proteins bind integrins without activating them., Here we define the structure of a complex between talin and the, membrane-proximal integrin beta3 cytoplasmic domain and identify specific, contacts between talin and the integrin tail required for activation. We, used structure-based mutagenesis to engineer talin and beta3 variants that, interact with comparable affinity to the wild-type proteins but inhibit, integrin activation by competing with endogenous talin. These results, reveal the structural basis of talin's unique ability to activate, integrins, identify an interaction that could aid in the design of, therapeutics to block integrin activation, and enable engineering of cells, with defects in the activation of multiple classes of integrins.
About this Structure
2H7E is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Structural basis of integrin activation by talin., Wegener KL, Partridge AW, Han J, Pickford AR, Liddington RC, Ginsberg MH, Campbell ID, Cell. 2007 Jan 12;128(1):171-82. PMID:17218263
Page seeded by OCA on Wed Nov 21 11:35:02 2007
