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Crystal Structure of the Catalytic Domain of Human Matrix Metalloproteinase 10
- Source :
- Journal of Molecular Biology. 336:707-716
- Publication Year :
- 2004
- Publisher :
- Elsevier BV, 2004.
-
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.
- Subjects :
- Models, Molecular
crystal structure
matrix metalloproteinase
Stereochemistry
Molecular Sequence Data
Crystal structure
Matrix (biology)
Matrix metalloproteinase
Crystallography, X-Ray
medicine.disease_cause
Catalysis
chemistry.chemical_compound
Matrix Metalloproteinase 10
Structural Biology
stromelysin-2
Catalytic Domain
Hydrolase
medicine
Humans
Amino Acid Sequence
Molecular Biology
Escherichia coli
Hydroxamic acid
Molecular Structure
Chemistry
Metalloendopeptidases
matrix metalloproteinase, stromelysin-2, MMP-10, crystal structure, inhibitor
Protein Structure, Tertiary
inhibitor
Stromelysin-2
MMP-10
Sequence Alignment
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 336
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Biology
- Accession number :
- edsair.doi.dedup.....13b13f25c7b2b583afe3b5c866d49fc8
- Full Text :
- https://doi.org/10.1016/j.jmb.2003.12.033