Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo.

Abstract

The integrin alphaLbeta2 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 alphaM and alpha2 subunits has been crystallized in both open and closed conformations; however, the… (More)

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Cite this paper

@article{Shimaoka2001ReversiblyLA, title={Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin alphaL I domains with high affinity and antagonist activity in vivo.}, author={Motomu Shimaoka and Chun Yu Lu and Roger T. Palframan and Ulrich H von Andrian and Aisling McCormack and Junichi Takagi and Timothy A Springer}, journal={Proceedings of the National Academy of Sciences of the United States of America}, year={2001}, volume={98 11}, pages={6009-14} }