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Article

A pivotal role for a conserved bulky residue at the α1-helix of the αI integrin domain in ligand binding.

The Journal of biological chemistry - 15 Dec 2017

Wang Zhengli, Thinn Aye Myat Myat, Zhu Jieqing

Abstract excerpt

The ligand-binding βI and αI domains of integrin are the best-studied von Willebrand factor A domains undergoing significant conformational changes for affinity regulation. In both βI and αI domains, the α1- and α7-helixes work in concert to shift the metal-ion-dependent adhesion site between the resting and active states. An absolutely conserved Gly in the middle of the α1-helix of βI helps maintain the resting...

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Source

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Identifiers

PMID: 29079572
DOI: 10.1074/jbc.M117.790519
PMCID: PMC5733610

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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