Functionally Important Interactions between the Nucleotide-Binding Domains of an Antigenic Peptide Transporter

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Functionally Important Interactions between the Nucleotide-Binding Domains of an Antigenic Peptide Transporter

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Title: Functionally Important Interactions between the Nucleotide-Binding Domains of an Antigenic Peptide Transporter
Author: Procko, Erik; Gaudet, Rachelle

Note: Order does not necessarily reflect citation order of authors.

Citation: Procko, Erik, and Rachelle Gaudet. 2008. Functionally important interactions between the nucleotide-binding domains of an antigenic peptide transporter. Biochemistry 47(21): 5699-5708.
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Abstract: The 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.
Published Version: doi:10.1021/bi7024854
Terms of Use: This article is made available under the terms and conditions applicable to Open Access Policy Articles, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#OAP
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:11169805
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