Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4934
Title: Crystal structure of the catalytic domain of human matrix metalloproteinase 10
Authors: I., Bertini
Calderone, Vito
M., Fragai
C., Luchinat
Mangani, Stefano 
Terni, B.
Keywords: matrix metalloproteinase, stromelysin-2, MMP-10, crystal structure, inhibitor
Issue Date: 2004
Project: None 
Journal: JOURNAL OF MOLECULAR BIOLOGY
Abstract: 
The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 A resolution. The availability of this structure allowed us to critically examine the small differences existing between the catalytic domains of MMP-3 and MMP-10, which show the highest sequence identity among all MMPs. Furthermore, the binding mode of N-isobutyl-N-[4-methoxyphenylsulfonyl] glycyl hydroxamic acid (NNGH), which is one of the most known commercial inhibitors of MMPs, is described for the first time.
Description: 
21806
URI: http://hdl.handle.net/20.500.12779/4934
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2003.12.033
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