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http://purl.uniprot.org/citations/23260142http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23260142http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23260142http://www.w3.org/2000/01/rdf-schema#comment"HLA-DR molecules bind microbial peptides in an endosomal compartment and present them on the cell surface for CD4 T cell surveillance. HLA-DM plays a critical role in the endosomal peptide selection process. The structure of the HLA-DM-HLA-DR complex shows major rearrangements of the HLA-DR peptide-binding groove. Flipping of a tryptophan away from the HLA-DR1 P1 pocket enables major conformational changes that position hydrophobic HLA-DR residues into the P1 pocket. These conformational changes accelerate peptide dissociation and stabilize the empty HLA-DR peptide-binding groove. Initially, incoming peptides have access to only part of the HLA-DR groove and need to compete with HLA-DR residues for access to the P2 site and the hydrophobic P1 pocket. This energetic barrier creates a rapid and stringent selection process for the highest-affinity binders. Insertion of peptide residues into the P2 and P1 sites reverses the conformational changes, terminating selection through DM dissociation."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2012.11.025"xsd:string
http://purl.uniprot.org/citations/23260142http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2012.11.025"xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Sethi D.K."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Sethi D.K."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Call M.J."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Call M.J."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Pyrdol J."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Pyrdol J."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Wucherpfennig K.W."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Wucherpfennig K.W."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Schulze M.S."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Schulze M.S."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Anders A.K."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Anders A.K."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Pos W."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/author"Pos W."xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/pages"1557-1568"xsd:string
http://purl.uniprot.org/citations/23260142http://purl.uniprot.org/core/pages"1557-1568"xsd:string