4CAK

Three-dimensional reconstruction of intact human integrin alphaIIbbeta3 in a phospholipid bilayer nanodisc

4CAK の概要

• エントリーDOI: 10.2210/pdb4cak/pdb
• EMDBエントリー: 2281
• 分子名称: Integrin alpha-IIb, Integrin beta-3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: cell adhesion, integrin, single particle reconstruction
• 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: 184314.93

構造登録者

Choi, W.S.,Rice, W.J.,Stokes, D.L.,Coller, B.S. (登録日: 2013-10-08, 公開日: 2013-10-30, 最終更新日: 2025-10-01)

主引用文献

Choi, W.S.,Rice, W.J.,Stokes, D.L.,Coller, B.S.
Three-Dimensional Reconstruction of Intact Human Integrin Alphaiibbeta3; New Implications for Activation-Dependent Ligand Binding.
Blood, 122:4165-, 2013

PubMed Abstract: Integrin αIIbβ3 plays a central role in hemostasis and thrombosis. We provide the first 3-dimensional reconstruction of intact purified αIIbβ3 in a nanodisc lipid bilayer. Unlike previous models, it shows that the ligand-binding head domain is on top, pointing away from the membrane. Moreover, unlike the crystal structure of the recombinant ectodomain, the lower legs are not parallel, straight, and adjacent. Rather, the αIIb lower leg is bent between the calf-1 and calf-2 domains and the β3 Integrin-Epidermal Growth Factor (I-EGF) 2 to 4 domains are freely coiled rather than in a cleft between the β3 headpiece and the αIIb lower leg. Our data indicate an important role for the region that links the distal calf-2 and β-tail domains to their respective transmembrane (TM) domains in transmitting the conformational changes in the TM domains associated with inside-out activation.

PubMed: 24136164
DOI: 10.1182/BLOOD-2013-04-499194

実験手法

ELECTRON MICROSCOPY (20.5 Å)