| http://purl.uniprot.org/citations/17036051 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17036051 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17036051 | http://www.w3.org/2000/01/rdf-schema#comment | "The human ATP-binding cassette (ABC) protein CFTR (cystic fibrosis transmembrane conductance regulator) is a chloride channel, whose dysfunction causes cystic fibrosis. To gain structural insight into the dynamic interaction between CFTR's nucleotide-binding domains (NBDs) proposed to underlie channel gating, we introduced target cysteines into the NBDs, expressed the channels in Xenopus oocytes, and used in vivo sulfhydryl-specific crosslinking to directly examine the cysteines' proximity. We tested five cysteine pairs, each comprising one introduced cysteine in the NH(2)-terminal NBD1 and another in the COOH-terminal NBD2. Identification of crosslinked product was facilitated by co-expression of NH(2)-terminal and COOH-terminal CFTR half channels each containing one NBD. The COOH-terminal half channel lacked all native cysteines. None of CFTR's 18 native cysteines was found essential for wild type-like, phosphorylation- and ATP-dependent, channel gating. The observed crosslinks demonstrate that NBD1 and NBD2 interact in a head-to-tail configuration analogous to that in homodimeric crystal structures of nucleotide-bound prokaryotic NBDs. CFTR phosphorylation by PKA strongly promoted both crosslinking and opening of the split channels, firmly linking head-to-tail NBD1-NBD2 association to channel opening."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.emboj.7601373"xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.emboj.7601373"xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Nairn A.C."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Nairn A.C."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Vergani P."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Vergani P."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Altberg G."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Altberg G."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Gadsby D.C."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Gadsby D.C."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Mense M."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "Mense M."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "White D.M."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/author | "White D.M."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/pages | "4728-4739"xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/pages | "4728-4739"xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/title | "In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer."xsd:string |
| http://purl.uniprot.org/citations/17036051 | http://purl.uniprot.org/core/title | "In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer."xsd:string |