2brq
From Proteopedia
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==Overview== | ==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 .. | + | 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 integrin-regulator talin, and these proteins compete for binding to integrin tails, allowing, integrin-filamin interactions to impact talin-dependent integrin, activation. Phosphothreonine-mimicking mutations inhibit filamin, but not, talin, binding, indicating that kinases may modulate this competition and, provide additional means to control integrin functions. |
==About this Structure== | ==About this Structure== | ||
| - | 2BRQ is a | + | 2BRQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GTT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BRQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:28:15 2007'' |
Revision as of 13:22, 5 November 2007
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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 integrin-regulator talin, and these proteins compete for binding to integrin tails, allowing, integrin-filamin interactions to impact talin-dependent integrin, activation. Phosphothreonine-mimicking mutations inhibit filamin, but not, talin, binding, indicating that kinases may modulate this competition and, provide additional means to control integrin functions.
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
Page seeded by OCA on Mon Nov 5 15:28:15 2007
Categories: Homo sapiens | Protein complex | Kiema, T.R. | Ylanne, J. | GOL | GTT | Actin-binding | Cell adhesion | Complex | Cytoskeleton | Filamin | Glycoprotein | Immunoglobulin like | Integrin | Receptor
