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http://purl.uniprot.org/citations/32161266http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32161266http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32161266http://www.w3.org/2000/01/rdf-schema#comment"Major Histocompatibility Complex (MHC) class I molecules selectively bind peptides for presentation to cytotoxic T cells. The peptide-free state of these molecules is not well understood. Here, we characterize a disulfide-stabilized version of the human class I molecule HLA-A*02:01 that is stable in the absence of peptide and can readily exchange cognate peptides. We present X-ray crystal structures of the peptide-free state of HLA-A*02:01, together with structures that have dipeptides bound in the A and F pockets. These structural snapshots reveal that the amino acid side chains lining the binding pockets switch in a coordinated fashion between a peptide-free unlocked state and a peptide-bound locked state. Molecular dynamics simulations suggest that the opening and closing of the F pocket affects peptide ligand conformations in adjacent binding pockets. We propose that peptide binding is co-determined by synergy between the binding pockets of the MHC molecule."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.org/dc/terms/identifier"doi:10.1038/s41467-020-14862-4"xsd:string
http://purl.uniprot.org/citations/32161266http://purl.org/dc/terms/identifier"doi:10.1038/s41467-020-14862-4"xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Meijers R."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Meijers R."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Zacharias M."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Zacharias M."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Hinrichs J."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Hinrichs J."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Springer S."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Springer S."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Uetrecht C."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Uetrecht C."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Anjanappa R."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Anjanappa R."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Garcia-Alai M."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Garcia-Alai M."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Aboelmagd M."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Aboelmagd M."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Kopicki J.D."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Kopicki J.D."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Lockhauserbaumer J."xsd:string
http://purl.uniprot.org/citations/32161266http://purl.uniprot.org/core/author"Lockhauserbaumer J."xsd:string