1m1x

From Proteopedia

Revision as of 14:21, 15 February 2008

CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+

Overview

The structural basis for the divalent cation-dependent binding of, heterodimeric alphabeta integrins to their ligands, which contain the, prototypical Arg-Gly-Asp sequence, is unknown. Interaction with ligands, triggers tertiary and quaternary structural rearrangements in integrins, that are needed for cell signaling. Here we report the crystal structure, of the extracellular segment of integrin alphaVbeta3 in complex with a, cyclic peptide presenting the Arg-Gly-Asp sequence. The ligand binds at, the major interface between the alphaV and beta3 subunits and makes, extensive contacts with both. Both tertiary and quaternary changes are, observed in the presence of ligand. The tertiary rearrangements take place, in betaA, the ligand-binding domain of beta3; in the complex, betaA, acquires two cations, one of which contacts the ligand Asp directly and, the other stabilizes the ligand-binding surface. Ligand binding induces, small changes in the orientation of alphaV relative to beta3.

Disease

Known diseases associated with this structure: Glanzmann thrombasthenia, type B OMIM:[173470]

About this Structure

1M1X is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand., Xiong JP, Stehle T, Zhang R, Joachimiak A, Frech M, Goodman SL, Arnaout MA, Science. 2002 Apr 5;296(5565):151-5. Epub 2002 Mar 7. PMID:11884718

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