1qc5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 20: | Line 20: | ||
[[Category: integrin]] | [[Category: integrin]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:59:19 2007'' | ||
Revision as of 16:54, 30 October 2007
|
I DOMAIN FROM INTEGRIN ALPHA1-BETA1
OverviewOverview
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 StructureAbout 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].
ReferenceReference
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
Page seeded by OCA on Tue Oct 30 15:59:19 2007