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...

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Dades bibliogràfiques

Publicat a:	Proc Natl Acad Sci U S A
Autors principals:	Lu, Chafen, Shimaoka, Motomu, Zang, Qun, Takagi, Junichi, Springer, Timothy A.
Format:	Artigo
Idioma:	Inglês
Publicat:	National Academy of Sciences 2001
Matèries:	Biological Sciences
Accés en línia:	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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