456c | pdb_0000456c
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CRYSTAL STRUCTURE OF COLLAGENASE-3 (MMP-13) COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID
Overview
The X-ray crystal structures of the catalytic domain of human, collagenase-3 (MMP-13) and collagenase-1 (MMP-1) with bound inhibitors, provides a basis for understanding the selectivity profile of a novel, series of matrix metalloprotease (MMP) inhibitors. Differences in the, relative size and shape of the MMP S1' pockets suggest that this pocket is, a critical determinant of MMP inhibitor selectivity. The collagenase-3 S1', pocket is long and open, easily accommodating large P1' groups, such as, diphenylether. In contrast, the collagenase-1 S1' pocket must undergo a, conformational change to accommodate comparable P1' groups. The, selectivity of the diphenylether series of inhibitors for collagenase-3 is, largely determined by their affinity for the preformed S1' pocket of, collagenase-3, as compared to the induced fit in collagenase-1.
About this Structure
456C is a Single protein structure of sequence from Homo sapiens with ZN, CA and CBP as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors., Lovejoy B, Welch AR, Carr S, Luong C, Broka C, Hendricks RT, Campbell JA, Walker KA, Martin R, Van Wart H, Browner MF, Nat Struct Biol. 1999 Mar;6(3):217-21. PMID:10074939
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