Structure of an allosteric inhibitor of LFA-1 bound to the I-domain studied by crystallography, NMR, and calorimetry.

Structure of an allosteric inhibitor of LFA-1 bound to the I-domain studied by crystallography, NMR, and calorimetry.

LFA-1 (lymphocyte function-associated antigen-1) plays a role in intercellular adhesion and lymphocyte trafficking and activation and is an attractive anti-inflammatory drug target. The alpha-subunit of LFA-1, in common with several other integrins, has an N-terminally inserted domain (I-domain) of...

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Main Authors: Crump, Matthew P (Author), Ceska, Thomas A (Author), Spyracopoulos, Leo (Author), Henry, Alistair (Author), Archibald, Sarah C (Author), Alexander, Rikki (Author), Taylor, Richard J (Author), Findlow, Stuart C. (Author), O'Connell, James (Author), Robinson, Martyn K (Author), Shock, Anthony (Author)
Format: Article
Language:English
Published: 2004-03-09.
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