http://purl.uniprot.org/citations/2176866 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2176866 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2176866 | http://www.w3.org/2000/01/rdf-schema#comment | "The complete amino acid sequence of the cyclic GMP stimulated cyclic nucleotide phosphodiesterase (cGS-PDE) of bovine heart has been determined by analysis of five digests of the protein; placement of the C-terminal 330 residues has been confirmed by interpretation of the corresponding partial cDNA clone. The holoenzyme is a homodimer of two identical N alpha-acetylated polypeptide chains of 921 residues, each with a calculated molecular weight of 103,244. The C-terminal region, residues 613-871, of the cGS-PDE comprises a catalytic domain that is conserved in all phosphodiesterase sequences except those of PDE 1 from Saccharomyces cerevisiae and a secreted PDE from Dictyostelium. A second conserved region, residues 209-567, is homologous to corresponding regions of the alpha and alpha' subunits of the photoreceptor phosphodiesterases. This conserved domain specifically binds cGMP and is involved in the allosteric regulation of the cGS-PDE. This regulatory domain contains two tandem, internal repeats, suggesting that it evolved from an ancestral gene duplication. Common cyclic nucleotide binding properties and a distant structural relationship provide evidence that the catalytic and regulatory domains within the cGS- and photoreceptor PDEs are also related by an ancient internal gene duplication."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00496a018"xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi00496a018"xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Walsh K.A."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Walsh K.A."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Beavo J.A."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Beavo J.A."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Charbonneau H."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Charbonneau H."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Sonnenburg W.K."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Sonnenburg W.K."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Stroop S.D."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Stroop S.D."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "le Trong H."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "le Trong H."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Beier N."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/author | "Beier N."xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/pages | "10280-10288"xsd:string |
http://purl.uniprot.org/citations/2176866 | http://purl.uniprot.org/core/pages | "10280-10288"xsd:string |