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-Structure paper
タイトル | Cryo-EM structure of the αvβ8 integrin reveals a mechanism for stabilizing integrin extension. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 25, Issue 8, Page 698-704, Year 2018 |
掲載日 | 2018年7月30日 |
著者 | Anthony Cormier / Melody G Campbell / Saburo Ito / Shenping Wu / Jianlong Lou / James Marks / Jody L Baron / Stephen L Nishimura / Yifan Cheng / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Struct Mol Biol / PubMed:30061598 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.8 Å |
構造データ | |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | MEMBRANE PROTEIN / GLYCOPROTEIN / ADHESION / FAB |