General structural features that regulate integrin affinity revealed by atypical αVβ8

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...

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Detalles Bibliográficos
Autores principales: Wang, Jianchuan, Su, Yang, Iacob, Roxana E., Engen, John R., Springer, Timothy A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6889490/
https://www.ncbi.nlm.nih.gov/pubmed/31792290
http://dx.doi.org/10.1038/s41467-019-13248-5

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6889490/
https://www.ncbi.nlm.nih.gov/pubmed/31792290
http://dx.doi.org/10.1038/s41467-019-13248-5

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