http://purl.uniprot.org/citations/24699645 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/24699645 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/24699645 | http://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/24699645 | http://purl.org/dc/terms/identifier | "doi:10.1107/s1399004714000078"xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.org/dc/terms/identifier | "doi:10.1107/s1399004714000078"xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Golinelli-Pimpaneau B."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Golinelli-Pimpaneau B."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Guimaraes B.G."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Guimaraes B.G."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Hamdane D."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Hamdane D."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Marden M.C."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Marden M.C."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Lechauve C."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/author | "Lechauve C."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/name | "Acta Crystallogr."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/name | "Acta Crystallogr."xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/pages | "1005-1014"xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/pages | "1005-1014"xsd:string |
http://purl.uniprot.org/citations/24699645 | http://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/24699645 | http://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/24699645 | http://purl.uniprot.org/core/volume | "70"xsd:string |
http://purl.uniprot.org/citations/24699645 | http://purl.uniprot.org/core/volume | "70"xsd:string |