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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...

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Autors principals: Shimaoka, Motomu, Lu, Chafen, Palframan, Roger T., von Andrian, Ulrich H., McCormack, Alison, Takagi, Junichi, Springer, Timothy A.
Format: Artigo
Idioma:Inglês
Publicat: The National Academy of Sciences 2001
Matèries:
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC33413/
https://ncbi.nlm.nih.gov/pubmed/11353828
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.101130498
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