1M1X

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

1M1X の概要

• エントリーDOI: 10.2210/pdb1m1x/pdb
• 関連するPDBエントリー: 1JV2 1M1U
• 分子名称: Integrin alpha-V, Integrin beta-3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: genu, hybrid domain, beta-tail domain, psi domain, egf domain, midas, admidas, cage motif, propeller, a-domain, thigh domain, calf domain, cell adhesion
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 186715.74

構造登録者

Xiong, J.-P.,Stehle, T.,Zhang, R.,Joachimiak, A.,Frech, M.,Goodman, S.L.,Arnaout, M.A. (登録日: 2002-06-20, 公開日: 2002-08-14, 最終更新日: 2024-10-16)

主引用文献

Xiong, J.P.,Stehle, T.,Zhang, R.,Joachimiak, A.,Frech, M.,Goodman, S.L.,Arnaout, M.A.
Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand.
Science, 296:151-155, 2002

PubMed Abstract: 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.

PubMed: 11884718
DOI: 10.1126/science.1069040

実験手法

X-RAY DIFFRACTION (3.3 Å)