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http://purl.uniprot.org/citations/8090713http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8090713http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8090713http://www.w3.org/2000/01/rdf-schema#comment"The X-ray crystal structure of a 19 kDa active fragment of human fibroblast collagenase has been determined by the multiple isomorphous replacement method and refined at 1.56 A resolution to an R-factor of 17.4%. The current structure includes a bound hydroxamate inhibitor, 88 waters and three metal atoms (two zincs and a calcium). The overall topology of the enzyme, comprised of a five stranded beta-sheet and three alpha-helices, is similar to the thermolysin-like metalloproteinases. There are some important differences between the collagenase and thermolysin families of enzymes. The active site zinc ligands are all histidines (His-218, His-222, and His-228). The presence of a second zinc ion in a structural role is a unique feature of the matrix metalloproteinases. The binding properties of the active site cleft are more dependent on the main chain conformation of the enzyme (and substrate) compared with thermolysin. A mechanism of action for peptide cleavage similar to that of thermolysin is proposed for fibroblast collagenase."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.org/dc/terms/identifier"doi:10.1002/prot.340190203"xsd:string
http://purl.uniprot.org/citations/8090713http://purl.org/dc/terms/identifier"doi:10.1002/prot.340190203"xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Vavra K.J."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Vavra K.J."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Wahl R.C."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Wahl R.C."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Johnson J.S."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Johnson J.S."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Et A.L."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Et A.L."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Spurlino J.C."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Spurlino J.C."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Banks T.M."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Banks T.M."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Carlton D.D."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Carlton D.D."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Cook E.R."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Cook E.R."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Falvo J."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Falvo J."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Pulvino T.A."xsd:string
http://purl.uniprot.org/citations/8090713http://purl.uniprot.org/core/author"Pulvino T.A."xsd:string