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http://purl.uniprot.org/SHA-384/874960C727E08E26E3AFE77BB8FD7B182D8E3C2A99395F5104B63FABCF19A3BE57D962C793B72B8E2DC4475F94788951http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/874960C727E08E26E3AFE77BB8FD7B182D8E3C2A99395F5104B63FABCF19A3BE57D962C793B72B8E2DC4475F94788951http://www.w3.org/2000/01/rdf-schema#comment"Models showed that congenital Glu(2.53(90))Lys and Glu(2.53(90))Asp mutations disrupt interactions with Ser(3.35(124)) and Trp(6.48(280)) respectively whereas the Glu(2.53(90))Arg and Trp(6.48(280))Arg mutations preserve intramolecular contacts but increase distance between the transmembrane helices. This disruption of interhelical contacts accounts for the effects of some disease-associated GnRH receptor mutations."xsd:string
http://purl.uniprot.org/uniprot/#_7436FFF6ADC8C9CCA62CD5505B63BFA464244C3B8CCD5B742138BA8C4413545287813949270F860D9E3887E69A5D35FBhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/874960C727E08E26E3AFE77BB8FD7B182D8E3C2A99395F5104B63FABCF19A3BE57D962C793B72B8E2DC4475F94788951
http://purl.uniprot.org/uniprot/P30968http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/874960C727E08E26E3AFE77BB8FD7B182D8E3C2A99395F5104B63FABCF19A3BE57D962C793B72B8E2DC4475F94788951
http://purl.uniprot.org/uniprot/#_P30968-mappedCitation-30476558http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/874960C727E08E26E3AFE77BB8FD7B182D8E3C2A99395F5104B63FABCF19A3BE57D962C793B72B8E2DC4475F94788951