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dc.contributor.authorProcko, Erik
dc.contributor.authorGaudet, Rachelle
dc.date.accessioned2013-10-15T13:59:40Z
dc.date.issued2008
dc.identifierQuick submit: 2013-07-15T11:32:25-04:00
dc.identifier.citationProcko, Erik, and Rachelle Gaudet. 2008. Functionally important interactions between the nucleotide-binding domains of an antigenic peptide transporter. Biochemistry 47(21): 5699-5708.en_US
dc.identifier.issn1990-7478en_US
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:11169805
dc.description.abstractThe transporter associated with antigen processing (TAP), an ABC transporter, pumps cytosolic peptides into the endoplasmic reticulum, where the peptides are loaded onto class I MHC molecules for presentation to the immune system. Transport is fueled by the binding of ATP to two cytosolic nucleotide-binding domains (NBDs) and ATP hydrolysis. We demonstrate biochemically that there are two electrostatic interactions across the interface between the two TAP NBDs and that these interactions are important for peptide transport. Notably, disrupting these interactions by mutagenesis does not greatly alter the ATP hydrolysis rate in an isolated NBD model system, suggesting that the interactions function at alternative stages in the transport cycle. The data support the general model for ABC transporters in which the NBDs form a tight, closed conformation during transport. Our results are discussed in relation to other ABC transporters that do or do not conserve potential interacting residues of opposite charges at the homologous positions.en_US
dc.description.sponsorshipMolecular and Cellular Biologyen_US
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.isversionofdoi:10.1021/bi7024854en_US
dash.licenseOAP
dc.titleFunctionally Important Interactions between the Nucleotide-Binding Domains of an Antigenic Peptide Transporteren_US
dc.typeJournal Articleen_US
dc.date.updated2013-07-15T15:32:55Z
dc.description.versionAccepted Manuscripten_US
dc.rights.holderErik Procko and Rachelle Gaudet
dc.relation.journalBiochemistryen_US
dash.depositing.authorGaudet, Rachelle
dc.identifier.doi10.1021/bi7024854*
workflow.legacycommentsIn QSDB.en_US
dash.contributor.affiliatedGaudet, Rachelle


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