Title of article :
Crystal Structure of the Catalytic Domain of Human Matrix Metalloproteinase 10
Author/Authors :
I. BERTINI، نويسنده , , V. Calderone، نويسنده , , M. Fragai، نويسنده , , C. Luchinat، نويسنده , , S. Mangani، نويسنده , , B. Terni، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2004
Pages :
10
From page :
707
To page :
716
Abstract :
The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 Å 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.
Keywords :
matrix metalloproteinase , stromelysin-2 , MMP-10 , crystal structure , Inhibitor
Journal title :
Journal of Molecular Biology
Serial Year :
2004
Journal title :
Journal of Molecular Biology
Record number :
1243399
Link To Document :
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