3ZE0

Integrin alphaIIB beta3 headpiece and RGD peptide complex

3ZE0 の概要

• エントリーDOI: 10.2210/pdb3ze0/pdb
• 関連するPDBエントリー: 3ZDX 3ZDY 3ZDZ 3ZE1 3ZE2
• 分子名称: INTEGRIN ALPHA-IIB, MANGANESE (II) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (13 entities in total)
• 機能のキーワード: cell adhesion-immune system-peptide complex, cell adhesion/immune system/peptide
• 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; Cell membrane; Single-pass type I membrane protein: P05106
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 302537.84

構造登録者

Zhu, J.H.,Zhu, J.Q.,Springer, T.A. (登録日: 2012-12-03, 公開日: 2013-06-05, 最終更新日: 2024-11-13)

主引用文献

Zhu, J.,Zhu, J.,Springer, T.A.
Complete Integrin Headpiece Opening in Eight Steps.
J.Cell Biol., 201:1053-, 2013

PubMed Abstract: Carefully soaking crystals with Arg-Gly-Asp (RGD) peptides, we captured eight distinct RGD-bound conformations of the αIIbβ3 integrin headpiece. Starting from the closed βI domain conformation, we saw six intermediate βI conformations and finally the fully open βI with the hybrid domain swung out in the crystal lattice. The β1-α1 backbone that hydrogen bonds to the Asp side chain of RGD was the first element to move followed by adjacent to metal ion-dependent adhesion site Ca(2+), α1 helix, α1' helix, β6-α7 loop, α7 helix, and hybrid domain. We define in atomic detail how conformational change was transmitted over long distances in integrins, 40 Å from the ligand binding site to the opposite end of the βI domain and 80 Å to the far end of the hybrid domain. During these movements, RGD slid in its binding groove toward αIIb, and its Arg side chain became ordered. RGD concentration requirements in soaking suggested a >200-fold higher affinity after opening. The thermodynamic cycle shows how higher affinity pays the energetic cost of opening.

PubMed: 23798730
DOI: 10.1083/JCB.201212037

実験手法

X-RAY DIFFRACTION (2.95 Å)