Locking in alternate conformations of the integrin αLβ2 I domain with disulfide bonds reveals functional relationships among integrin domains
We used integrin αLβ2 heterodimers containing I domains locked open (active) or closed (inactive) with disulfide bonds to investigate regulatory interactions among domains in integrins. mAbs to the αL I domain and β2 I-like domain inhibit adhesion of wild-type αLβ2 to intercellular adhesion molecule...
Gorde:
| Argitaratua izan da: | Proc Natl Acad Sci U S A |
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| Egile Nagusiak: | , , , , |
| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
National Academy of Sciences
2001
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| Gaiak: | |
| Sarrera elektronikoa: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC30149/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11226250/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.041618598 |
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