6DJP

Integrin alpha-v beta-8 in complex with the Fabs 8B8 and 68

6DJP の概要

• エントリーDOI: 10.2210/pdb6djp/pdb
• EMDBエントリー: 7939
• 分子名称: Integrin alpha-v, 2-acetamido-2-deoxy-beta-D-glucopyranose, Integrin beta-8, ... (10 entities in total)
• 機能のキーワード: glycoprotein, membrane protein, adhesion, fab
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 274901.35

構造登録者

Cormier, A.,Campbell, M.G.,Nishimura, S.L.,Cheng, Y. (登録日: 2018-05-25, 公開日: 2018-07-25, 最終更新日: 2024-10-09)

主引用文献

Cormier, A.,Campbell, M.G.,Ito, S.,Wu, S.,Lou, J.,Marks, J.,Baron, J.L.,Nishimura, S.L.,Cheng, Y.
Cryo-EM structure of the alpha v beta 8 integrin reveals a mechanism for stabilizing integrin extension.
Nat. Struct. Mol. Biol., 25:698-704, 2018

PubMed Abstract: Integrins are conformationally flexible cell surface receptors that survey the extracellular environment for their cognate ligands. Interactions with ligands are thought to be linked to global structural rearrangements involving transitions between bent, extended-closed and extended-open forms. Thus far, structural details are lacking for integrins in the extended conformations due to extensive flexibility between the headpiece and legs in this conformation. Here we present single-particle electron cryomicroscopy structures of human αvβ8 integrin in the extended-closed conformation, which has been considered to be a low-affinity intermediate. Our structures show the headpiece rotating about a flexible αv knee, suggesting a ligand surveillance mechanism for integrins in their extended-closed form. Our model predicts that the extended conformation is mainly stabilized by an interface formed between flexible loops in the upper and lower domains of the αv leg. Confirming these findings with the αvβ3 integrin suggests that our model of stabilizing the extended-closed conformation is generalizable to other integrins.

PubMed: 30061598
DOI: 10.1038/s41594-018-0093-x

実験手法

ELECTRON MICROSCOPY (4.8 Å)