1M8O

Platelet integrin alfaIIb-beta3 cytoplasmic domain

1M8O の概要

• エントリーDOI: 10.2210/pdb1m8o/pdb
• 分子名称: platelet integrin alfaIIb subunit: cytoplasmic domain, platelet integrin beta3 subunit: cytoplasmic domain (2 entities in total)
• 機能のキーワード: alfa helix, platelet, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P08514 P05106
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 7981.85

構造登録者

Vinogradova, O.,Velyvis, A.,Velyviene, A.,Hu, B.,Haas, T.,Plow, E.F.,Qin, J. (登録日: 2002-07-25, 公開日: 2002-09-18, 最終更新日: 2024-05-22)

主引用文献

Vinogradova, O.,Velyvis, A.,Velyviene, A.,Hu, B.,Haas, T.A.,Plow, E.F.,Qin, J.
A Structural mechanism of integrin alfaiib beta3 "Inside-out" Activation as regulated by its cytoplasmic face.
Cell(Cambridge,Mass.), 110:587-597, 2002

PubMed Abstract: Activation of the ligand binding function of integrin heterodimers requires transmission of an "inside-out" signal from their small intracellular segments to their large extracellular domains. The structure of the cytoplasmic domain of a prototypic integrin alpha(IIb)beta(3) has been solved by NMR and reveals multiple hydrophobic and electrostatic contacts within the membrane-proximal helices of its alpha and the beta cytoplasmic tails. The interface interactions are disrupted by point mutations or the cytoskeletal protein talin that are known to activate the receptor. These results provide a structural mechanism by which a handshake between the alpha and the beta cytoplasmic tails restrains the integrin in a resting state and unclasping of this interaction triggers the inside-out conformational signal that leads to receptor activation.

PubMed: 12230976
DOI: 10.1016/S0092-8674(02)00906-6

実験手法

SOLUTION NMR