Structure of an Allosteric Inhibitor of LFA-1 Bound to the I-Domain Studied by Crystallography, NMR, and Calorimetry,-Reference-Cited by-同舟云学术

Structure of an Allosteric Inhibitor of LFA-1 Bound to the I-Domain Studied by Crystallography, NMR, and Calorimetry,

Published:2004-02-13 Issue:9 Volume:43 Page:2394-2404
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Crump Matthew P.¹,Ceska Thomas A.¹,Spyracopoulos Leo¹,Henry Alistair¹,Archibald Sarah C.¹,Alexander Rikki¹,Taylor Richard J.¹,Findlow Stuart C.¹,O'Connell James¹,Robinson Martyn K.¹,Shock Anthony¹

Affiliation:

1. School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, U.K., Celltech R&D, 216 Bath Road, Slough, Berks SL1 4EN, U.K., and MRC Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi035422a

Reference46 articles.

1. Conformational Regulation of Integrin Structure and Function

2. The role of leukocyte function-associated antigen-1 in animal models of inflammation

3. Lymphocyte Migration in Lymphocyte Function-associated Antigen (LFA)-1–deficient Mice

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