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An isolated, surface-expressed I domain of the integrin αLβ2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond
We introduced disulfide bonds to lock the integrin αLβ2 I domain in predicted open, ligand binding or closed, nonbinding conformations. Transfectants expressing αLβ2 heterodimers containing locked-open but not locked-closed or wild-type I domains constitutively adhered to intercellular adhesion mole...
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| Autori principali: | , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
The National Academy of Sciences
2001
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC30148/ https://ncbi.nlm.nih.gov/pubmed/11226249 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.041606398 |
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