General structural features that regulate integrin affinity revealed by atypical αVβ8

• Published in: Nature communications Vol. 10; no. 1; pp. 5481 - 13
• Main Authors: Wang, Jianchuan, Su, Yang, Iacob, Roxana E, Engen, John R, Springer, Timothy A
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 02.12.2019; Nature Publishing Group UK; Nature Portfolio
• Subjects: Affinity; Amino Acid Sequence; BASIC BIOLOGICAL SCIENCES; Binding Sites; Cations; Cell signalling; Conformation; Coupling; Crystal structure; Cytoskeleton; Deuterium; Divalent cations; Domains; Helices; Humans; Hydrogen-deuterium exchange; Integrin beta Chains - chemistry; Integrin beta Chains - genetics; Integrin beta Chains - metabolism; Integrins; Integrins - chemistry; Integrins - genetics; Integrins - metabolism; Ligands; Mass spectrometry; Mutants; Protein Domains; Protein Structure, Secondary; Sequence Alignment; X-ray crystallography

Integrin αVβ8, which like αVβ6 functions to activate TGF-βs, is atypical. Its β8 subunit binds to a distinctive cytoskeleton adaptor and does not exhibit large changes in conformation upon binding to ligand. Here, crystal structures, hydrogen-deuterium exchange dynamics, and affinity measurements on...