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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Detalles Bibliográficos
Main Authors: Lu, Chafen, Shimaoka, Motomu, Zang, Qun, Takagi, Junichi, Springer, Timothy A.
Formato: Artigo
Idioma:Inglês
Publicado: The National Academy of Sciences 2001
Assuntos:
Biological Sciences
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC30149/
https://ncbi.nlm.nih.gov/pubmed/11226250
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.041618598
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