1BR9

HUMAN TISSUE INHIBITOR OF METALLOPROTEINASE-2

Summary for 1BR9

• Entry DOI: 10.2210/pdb1br9/pdb
• Descriptor: METALLOPROTEINASE-2 INHIBITOR (2 entities in total)
• Functional Keywords: proteinase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P16035
• Total number of polymer chains: 1
• Total formula weight: 21783.04

Authors

Tuuttila, A.,Morgunova, E.,Bergmann, U.,Lindqvist, Y.,Tryggvason, K.,Schneider, G. (deposition date: 1998-08-28, release date: 1999-05-04, Last modification date: 2024-10-16)

Primary citation

Tuuttila, A.,Morgunova, E.,Bergmann, U.,Lindqvist, Y.,Maskos, K.,Fernandez-Catalan, C.,Bode, W.,Tryggvason, K.,Schneider, G.
Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution.
J.Mol.Biol., 284:1133-1140, 1998

PubMed Abstract: 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.

PubMed: 9837731
DOI: 10.1006/jmbi.1998.2223

Experimental method

X-RAY DIFFRACTION (2.1 Å)