1br9
|
HUMAN TISSUE INHIBITOR OF METALLOPROTEINASE-2
OverviewOverview
The three-dimensional structure of human tissue inhibitor of, metalloproteinases-2 (TIMP-2) was determined by X-ray crystallography to, 2.1 A resolution. The structure of the inhibitor consists of two domains., The N-terminal domain (residues 1-110) is folded into a beta-barrel, similar to the oligonucleotide/oligosaccharide binding fold otherwise, found in certain DNA-binding proteins. The C-terminal domain (residues, 111-194) contains a parallel stranded beta-hairpin plus a beta-loop-beta, motif. Comparison of the structure of uncomplexed human TIMP-2 with that, of bovine TIMP-2 bound to the catalytic domain of human MMP-14 suggests an, internal rotation between the two domains of approximately 13 degrees upon, binding to the protease. Furthermore, local conformational differences in, the two structures that might be induced by formation of the, protease-inhibitor complex have been found. The most prominent of these, involves residues 27-40 of the A-B beta-hairpin loop. Structure-based, alignment of amino acid sequences of representatives of the TIMP family, maps the sequence differences mainly to loop regions, and some of these, differences are proposed to be responsible for the particular properties, of the various TIMP species.
About this StructureAbout this Structure
1BR9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution., Tuuttila A, Morgunova E, Bergmann U, Lindqvist Y, Maskos K, Fernandez-Catalan C, Bode W, Tryggvason K, Schneider G, J Mol Biol. 1998 Dec 11;284(4):1133-40. PMID:9837731
Page seeded by OCA on Mon Nov 12 16:13:50 2007