Functionally Important Interactions between the Nucleotide-Binding Domains of an Antigenic Peptide Transporter
Author:
Affiliation:
1. Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts 02138
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi7024854
Reference31 articles.
1. Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
2. Identification of domain boundaries within the N‐termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin‐mediated increase in peptide loading of MHC class I
3. Structure and Function of ABC Transporters
4. Structural Biology of Rad50 ATPase
5. ATP Binding to the Motor Domain from an ABC Transporter Drives Formation of a Nucleotide Sandwich Dimer
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2. New insights into the structure of the MHC class I peptide-loading complex and mechanisms of TAP inhibition by viral immune evasion proteins;Molecular Immunology;2019-09
3. D-helix influences dimerization of the ATP-binding cassette (ABC) transporter associated with antigen processing 1 (TAP1) nucleotide-binding domain;PLOS ONE;2017-05-23
4. Type I Protein Secretion—Deceptively Simple yet with a Wide Range of Mechanistic Variability across the Family;EcoSal Plus;2016-01-11
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