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http://purl.uniprot.org/citations/7918391http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7918391http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7918391http://www.w3.org/2000/01/rdf-schema#comment"Homonuclear two-dimensional and three-dimensional 1H nuclear magnetic resonance spectroscopy has been used to obtain essentially complete sequence-specific assignments for 123 of the 127 amino acid residues present in the truncated form of tissue inhibitor of metalloproteinases-2 (delta TIMP-2), the active N-terminal domain of the protein. Analysis of the through-space nuclear Overhauser effect data obtained for delta TIMP-2 allowed determination of both the secondary structure of the domain and also a low-resolution tertiary structure defining the protein backbone topology. The protein contains a five-stranded antiparallel beta-sheet that is rolled over on itself to form a closed beta-barrel, and two short helices which pack close to one another on the same barrel face. A comparison of the delta TIMP-2 structure with other known protein folds reveals that the beta-barrel topology is homologous to that seen in proteins of the oligosaccharide/oligonucleotide binding (OB) fold family. The common structural features include the number of beta-strands and their arrangement, the beta-barrel shear number, an interstrand hydrogen bond network, the packing of the hydrophobic core, and a conserved beta-bulge. Superpositions of the beta-barrels from delta TIMP-2 and two previously known members of the OB protein fold family (staphylococcal nuclease and Escherichia coli heat-labile enterotoxin) confirmed the similarity in beta-barrel topology. The three-dimensional structure of delta TIMP-2 has allowed a more detailed interpretation than was previously possible of the functional significance of available protein sequence and site-directed mutagenesis data for the TIMP family. Furthermore, the structure has revealed conserved surface regions of potential functional importance."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.org/dc/terms/identifier"doi:10.1021/bi00205a010"xsd:string
http://purl.uniprot.org/citations/7918391http://purl.org/dc/terms/identifier"doi:10.1021/bi00205a010"xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Murphy G."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Murphy G."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Feeney J."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Feeney J."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Freedman R.B."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Freedman R.B."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Carr M.D."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Carr M.D."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Williamson R.A."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Williamson R.A."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Martorell G."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Martorell G."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Docherty A.J.P."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/author"Docherty A.J.P."xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/pages"11745-11759"xsd:string
http://purl.uniprot.org/citations/7918391http://purl.uniprot.org/core/pages"11745-11759"xsd:string