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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...
Αποθηκεύτηκε σε:
| Τόπος έκδοσης: | Nat Commun |
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| Κύριοι συγγραφείς: | , , , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
Nature Publishing Group UK
2019
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| Θέματα: | |
| Διαθέσιμο Online: | 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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