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http://purl.uniprot.org/citations/26988023http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26988023http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26988023http://www.w3.org/2000/01/rdf-schema#comment"Progesterone-receptor membrane component 1 (PGRMC1/Sigma-2 receptor) is a haem-containing protein that interacts with epidermal growth factor receptor (EGFR) and cytochromes P450 to regulate cancer proliferation and chemoresistance; its structural basis remains unknown. Here crystallographic analyses of the PGRMC1 cytosolic domain at 1.95 Å resolution reveal that it forms a stable dimer through stacking interactions of two protruding haem molecules. The haem iron is five-coordinated by Tyr113, and the open surface of the haem mediates dimerization. Carbon monoxide (CO) interferes with PGRMC1 dimerization by binding to the sixth coordination site of the haem. Haem-mediated PGRMC1 dimerization is required for interactions with EGFR and cytochromes P450, cancer proliferation and chemoresistance against anti-cancer drugs; these events are attenuated by either CO or haem deprivation in cancer cells. This study demonstrates protein dimerization via haem-haem stacking, which has not been seen in eukaryotes, and provides insights into its functional significance in cancer."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.org/dc/terms/identifier"doi:10.1038/ncomms11030"xsd:string
http://purl.uniprot.org/citations/26988023http://purl.org/dc/terms/identifier"doi:10.1038/ncomms11030"xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Kobayashi T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Kobayashi T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Yamamoto T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Yamamoto T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Uchida T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Uchida T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Uchiyama S."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Uchiyama S."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Iwata S."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Iwata S."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Nakane T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Nakane T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Shimamura T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Shimamura T."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Yamamoto A."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Yamamoto A."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Ishimori K."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Ishimori K."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Koike I."xsd:string
http://purl.uniprot.org/citations/26988023http://purl.uniprot.org/core/author"Koike I."xsd:string