http://purl.uniprot.org/citations/19648278 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19648278 | http://www.w3.org/2000/01/rdf-schema#comment | "Peptide binding to class II MHC protein is commonly viewed as a combination of discrete anchor residue preferences for pockets 1, 4, 6/7, and 9. However, previous studies have suggested cooperative effects during the peptide binding process. Investigation of the DRB1*0901 binding motif demonstrated a clear interaction between peptide binding pockets 6 and 9. In agreement with prior studies, pockets 1 and 4 exhibited clear binding preferences. Previously uncharacterized pockets 6 and 7 accommodated a wide variety of residues. However, although it was previously reported that pocket 9 is completely permissive, several substitutions at this position were unable to bind. Structural modeling revealed a probable interaction between pockets 6 and 9 through beta9Lys. Additional binding studies with doubly substituted peptides confirmed that the amino acid bound within pocket 6 profoundly influences the binding preferences for pocket 9 of DRB1*0901, causing complete permissiveness of pocket 9 when a small polar residue is anchored in pocket 6 but accepting relatively few residues when a basic residue is anchored in pocket 6. The beta9Lys residue is unique to DR9 alleles. However, similar studies with doubly substituted peptides confirmed an analogous interaction effect for DRA1/B1*0301, a beta9Glu allele. Accounting for this interaction resulted in improved epitope prediction. These findings provide a structural explanation for observations that an amino acid in one pocket can influence binding elsewhere in the MHC class II peptide binding groove."xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.org/dc/terms/identifier | "doi:10.4049/jimmunol.0802228"xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/author | "Kwok W.W."xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/author | "James E.A."xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/author | "Moustakas A.K."xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/author | "Papadopoulos G.K."xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/author | "Bui J."xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/author | "Nouv R."xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/pages | "3249-3258"xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/title | "The binding of antigenic peptides to HLA-DR is influenced by interactions between pocket 6 and pocket 9."xsd:string |
http://purl.uniprot.org/citations/19648278 | http://purl.uniprot.org/core/volume | "183"xsd:string |
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