1rm8

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spinqualitylabelsall models 1rm8, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features

Overview

Membrane-type matrix metalloproteinases (MT-MMPs) have attracted strong, attention, because four of them can activate a key player in the tumor, scenario, proMMP-2/progelatinase A. In addition to this indirect effect on, the cellular environment, these MT-MMPs degrade extracellular matrix, proteins, and their overproduction is associated with tumor growth. We, have solved the structure of the catalytic domain (cd) of MT3-MMP/MMP-16, in complex with the hydroxamic acid inhibitor batimastat. CdMT3-MMP, exhibits a classical MMP-fold with similarity to MT1-MMP. Nevertheless, it, also shows unique properties such as a modified MT-specific loop and a, closed S1' specificity pocket, which might help to design specific, inhibitors. Some MT-MMP-specific features, derived from the crystal, structures of MT-1-MMP determined previously and MT3-MMP, and revealed in, recent mutagenesis experiments, explain the impaired interaction of the, MT-MMPs with TIMP-1. Docking experiments with proMMP-2 show some exposed, loops including the MT-loop of cdMT3-MMP involved in the interaction with, the proMMP-2 prodomain in the activation encounter complex. This model, might help to understand the experimentally proven importance of the, MT-loop for the activation of proMMP-2.

About this Structure

1RM8 is a Single protein structure of sequence from Homo sapiens with ZN, CA and BAT as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features., Lang R, Braun M, Sounni NE, Noel A, Frankenne F, Foidart JM, Bode W, Maskos K, J Mol Biol. 2004 Feb 6;336(1):213-25. PMID:14741217

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