2brq

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[[Category: receptor]]
[[Category: receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:25:18 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:46:19 2007''

Revision as of 14:41, 30 October 2007


2brq, resolution 2.10Å

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CRYSTAL STRUCTURE OF THE FILAMIN A REPEAT 21 COMPLEXED WITH THE INTEGRIN BETA7 CYTOPLASMIC TAIL PEPTIDE

Overview

The ability of adhesion receptors to transmit biochemical signals and, mechanical force across cell membranes depends on interactions with the, actin cytoskeleton. Filamins are large, actin-crosslinking proteins that, connect multiple transmembrane and signaling proteins to the cytoskeleton., Here, we describe the high-resolution structure of an interface between, filamin A and an integrin adhesion receptor. When bound, the integrin beta, cytoplasmic tail forms an extended beta strand that interacts with beta, strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This, interface is common to many integrins, and we suggest it is a prototype, for other IgFLN domain interactions. Notably, the structurally defined, filamin binding site overlaps with that of the ... [(full description)]

About this Structure

2BRQ is a [Protein complex] structure of sequences from [Homo sapiens] with GTT and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The molecular basis of filamin binding to integrins and competition with talin., Kiema T, Lad Y, Jiang P, Oxley CL, Baldassarre M, Wegener KL, Campbell ID, Ylanne J, Calderwood DA, Mol Cell. 2006 Feb 3;21(3):337-47. PMID:16455489

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