1L3Y

INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 SUBUNIT

1L3Y の概要

• エントリーDOI: 10.2210/pdb1l3y/pdb
• NMR情報: BMRB: 5338
• 分子名称: Integrin beta-2:CYSTEINE-RICH MODULE 3 (1 entity in total)
• 機能のキーワード: integrin, beta-2 subunit, cell adhesion, cysteine-rich module, egf-like module
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P05107
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4332.91

構造登録者

Beglova, N.,Blacklow, S.C.,Takagi, J.,Springer, T.A. (登録日: 2002-03-03, 公開日: 2002-04-01, 最終更新日: 2024-11-20)

主引用文献

Beglova, N.,Blacklow, S.C.,Takagi, J.,Springer, T.A.
Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation.
Nat.Struct.Biol., 9:282-287, 2002

PubMed Abstract: Cysteine-rich repeats in the integrin beta subunit stalk region relay activation signals to the ligand-binding headpiece. The NMR solution structure and disulfide bond connectivity of Cys-rich module-3 of the integrin beta2 subunit reveal a nosecone-shaped variant of the EGF fold, termed an integrin-EGF (I-EGF) domain. Interdomain contacts between I-EGF domains 2 and 3 observed by NMR support a model in which the modules are related by an approximate two-fold screw axis in an extended arrangement. Our findings complement a 3.1 A crystal structure of the extracellular portion of integrin alphaVbeta3, which lacks an atomic model for I-EGF2 and a portion of I-EGF3. The disulfide connectivity of I-EGF3 chemically assigned here differs from the pairings suggested in the alphaVbeta3 structure. Epitopes that become exposed upon integrin activation and residues that restrain activation are defined in beta2 I-EGF domains 2 and 3. Superposition on the alphaVbeta3 structure reveals that they are buried. This observation suggests that the highly bent alphaVbeta3 structure represents the inactive conformation and that release of contacts with I-EGF modules 2 and 3 triggers a switchblade-like opening motion extending the integrin into its active conformation.

PubMed: 11896403
DOI: 10.1038/nsb779

実験手法

SOLUTION NMR