Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin αL I domains with high affinity and antagonist activity in vivo
The integrin αLβ2 has three different domains in its headpiece that have been suggested to either bind ligand or to regulate ligand binding. One of these, the inserted or I domain, has a fold similar to that of small G proteins. The I domain of the αM and α2 subunits has been crystallized in both op...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2001
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC33413/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11353828/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.101130498 |
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