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http://purl.uniprot.org/citations/10074346http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10074346http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10074346http://www.w3.org/2000/01/rdf-schema#comment"The structure of fragment double-D from human fibrin has been solved in the presence and absence of the peptide ligands that simulate the two knobs exposed by the removal of fibrinopeptides A and B, respectively. All told, six crystal structures have been determined, three of which are reported here for the first time: namely, fragments D and double-D with the peptide GHRPam alone and double-D in the absence of any peptide ligand. Comparison of the structures has revealed a series of conformational changes that are brought about by the various knob-hole interactions. Of greatest interest is a moveable "flap" of two negatively charged amino acids (Glubeta397 and Aspbeta398) whose side chains are pinned back to the coiled coil with a calcium atom bridge until GHRPam occupies the beta-chain pocket. Additionally, in the absence of the peptide ligand GPRPam, GHRPam binds to the gamma-chain pocket, a new calcium-binding site being formed concomitantly."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.org/dc/terms/identifier"doi:10.1021/bi982626w"xsd:string
http://purl.uniprot.org/citations/10074346http://purl.org/dc/terms/identifier"doi:10.1021/bi982626w"xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/author"Spraggon G."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/author"Spraggon G."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/author"Doolittle R.F."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/author"Doolittle R.F."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/author"Everse S.J."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/author"Everse S.J."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/author"Veerapandian L."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/author"Veerapandian L."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/pages"2941-2946"xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/pages"2941-2946"xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/title"Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/title"Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide."xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/volume"38"xsd:string
http://purl.uniprot.org/citations/10074346http://purl.uniprot.org/core/volume"38"xsd:string
http://purl.uniprot.org/citations/10074346http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10074346
http://purl.uniprot.org/citations/10074346http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10074346