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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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| Publicat a: | Nat Commun |
|---|---|
| Autors principals: | , , , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Nature Publishing Group UK
2019
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6889490/ https://ncbi.nlm.nih.gov/pubmed/31792290 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-019-13248-5 |
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