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http://purl.uniprot.org/citations/24699645http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24699645http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24699645http://www.w3.org/2000/01/rdf-schema#comment"Neuroglobin plays an important function in the supply of oxygen in nervous tissues. In human neuroglobin, a cysteine at position 46 in the loop connecting the C and D helices of the globin fold is presumed to form an intramolecular disulfide bond with Cys55. Rupture of this disulfide bridge stabilizes bi-histidyl haem hexacoordination, causing an overall decrease in the affinity for oxygen. Here, the first X-ray structure of wild-type human neuroglobin is reported at 1.74 Å resolution. This structure provides a direct observation of two distinct conformations of the CD region containing the intramolecular disulfide link and highlights internal cavities that could be involved in ligand migration and/or are necessary to enable the conformational transition between the low and high oxygen-affinity states following S-S bond formation."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.org/dc/terms/identifier"doi:10.1107/s1399004714000078"xsd:string
http://purl.uniprot.org/citations/24699645http://purl.org/dc/terms/identifier"doi:10.1107/s1399004714000078"xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Golinelli-Pimpaneau B."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Golinelli-Pimpaneau B."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Guimaraes B.G."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Guimaraes B.G."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Hamdane D."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Hamdane D."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Marden M.C."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Marden M.C."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Lechauve C."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/author"Lechauve C."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/name"Acta Crystallogr."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/name"Acta Crystallogr."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/pages"1005-1014"xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/pages"1005-1014"xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/title"The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/title"The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity."xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/volume"70"xsd:string
http://purl.uniprot.org/citations/24699645http://purl.uniprot.org/core/volume"70"xsd:string