9P97

CryoEM structure of the closed integrin alphaEbeta7 bound to fab LF61

9P97 の概要

• エントリーDOI: 10.2210/pdb9p97/pdb
• EMDBエントリー: 71401
• 分子名称: Integrin alpha-E, Integrin beta-7, Fab LF61 Heavy Chain, ... (9 entities in total)
• 機能のキーワード: aeb7, gut adhesion, tissue residence, membrane receptor, cell adhesion
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 264813.20

構造登録者

Hollis, J.A.,Campbell, M.G. (登録日: 2025-06-24, 公開日: 2025-09-24)

主引用文献

Hollis, J.A.,Chan, M.C.,Malik, H.S.,Campbell, M.G.
Molecular exaptation by the integrin alpha I domain.
Sci Adv, 11:eadx9567-eadx9567, 2025

PubMed Abstract: Integrins bind ligands between their alpha (α) and beta (β) subunits and transmit signals through conformational changes. Early in chordate evolution, some α subunits acquired an "inserted" (I) domain that expanded integrin's ligand-binding repertoire but obstructed the ancestral ligand pocket, seemingly blocking conventional integrin activation. Here, we compare cryo-electron microscopy structures of apo and ligand-bound states of the I domain-containing αEβ integrin and the I domain-lacking αβ integrin to illuminate how the I domain intrinsically mimics an extrinsic ligand to preserve integrin function. We trace the I domain's evolutionary origin to an ancestral collagen-collagen interaction domain, identifying an ancient molecular exaptation that facilitated integrin activation immediately upon I domain insertion. Our analyses reveal the evolutionary and biochemical basis of expanded cellular communication in vertebrates.

PubMed: 40929264
DOI: 10.1126/sciadv.adx9567

実験手法

ELECTRON MICROSCOPY (2.92 Å)