1qc5

From Proteopedia

Revision as of 13:54, 30 October 2007

I DOMAIN FROM INTEGRIN ALPHA1-BETA1

Overview

Most mammalian cells and some pathogenic bacteria are capable of adhering, to collagenous substrates in processes mediated by specific cell surface, adherence molecules. Crystal structures of collagen-binding regions of the, human integrin alpha(2)beta(1) and a Staphylococcus aureus adhesin reveal, a "trench" on the surface of both of these proteins. This trench can, accommodate a collagen triple-helical structure and presumably represents, the ligand-binding site (Emsley, J., King, S. L., Bergelson, J. M., and, Liddington, R. C. (1997) J. Biol. Chem. 272, 28512-28517; Symersky, J., Patti, J. M., Carson, M., House-Pompeo, K., Teale, M., Moore, D., Jin, L., Schneider, A., DeLucas, L. J., Hook, M., and Narayana, S. V. L. (1997), Nat. Struct. Biol. 4, 833-838). We report here the crystal ... [(full description)]

About this Structure

1QC5 is a [Protein complex] structure of sequences from [Homo sapiens] with MG as [ligand]. Structure known Active Site: MGA. Full crystallographic information is available from [OCA].

Reference

Trench-shaped binding sites promote multiple classes of interactions between collagen and the adherence receptors, alpha(1)beta(1) integrin and Staphylococcus aureus cna MSCRAMM., Rich RL, Deivanayagam CC, Owens RT, Carson M, Hook A, Moore D, Symersky J, Yang VW, Narayana SV, Hook M, J Biol Chem. 1999 Aug 27;274(35):24906-13. PMID:10455165

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