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Article

Dynamics of integrin α5β1, fibronectin, and their complex reveal sites of interaction and conformational change.

The Journal of biological chemistry - 1 Sept 2022

Su Yang, Iacob Roxana E, Li Jing, Engen John R, Springer Timothy A

Abstract excerpt

Integrin α5β1 mediates cell adhesion to the extracellular matrix by binding fibronectin (Fn). Selectivity for Fn by α5β1 is achieved through recognition of an RGD motif in the 10th type III Fn domain (Fn10) and the synergy site in the ninth type III Fn domain (Fn9). However, details of the interaction dynamics are unknown. Here, we compared synergy-site and Fn-truncation mutations for their α5β1-binding...

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Identifiers

PMID: 35931112
DOI: 10.1016/j.jbc.2022.102323
PMCID: PMC9483561

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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