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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1996-2-22
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pubmed:abstractText |
In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
378
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
126-30
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8549817-Amino Acid Sequence,
pubmed-meshheading:8549817-Animals,
pubmed-meshheading:8549817-Binding Sites,
pubmed-meshheading:8549817-Crystallization,
pubmed-meshheading:8549817-Crystallography, X-Ray,
pubmed-meshheading:8549817-Electrochemistry,
pubmed-meshheading:8549817-Gelatinases,
pubmed-meshheading:8549817-Hemopexin,
pubmed-meshheading:8549817-Humans,
pubmed-meshheading:8549817-Matrix Metalloproteinase 2,
pubmed-meshheading:8549817-Metalloendopeptidases,
pubmed-meshheading:8549817-Models, Molecular,
pubmed-meshheading:8549817-Molecular Sequence Data,
pubmed-meshheading:8549817-Molecular Structure,
pubmed-meshheading:8549817-Peptide Fragments,
pubmed-meshheading:8549817-Protease Inhibitors,
pubmed-meshheading:8549817-Protein Structure, Secondary,
pubmed-meshheading:8549817-Proteins,
pubmed-meshheading:8549817-Sequence Homology,
pubmed-meshheading:8549817-Structure-Activity Relationship,
pubmed-meshheading:8549817-Swine,
pubmed-meshheading:8549817-Tissue Inhibitor of Metalloproteinase-2
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pubmed:year |
1996
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pubmed:articleTitle |
The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.
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pubmed:affiliation |
Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Martinsried bei München, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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