| http://purl.uniprot.org/citations/7667286 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7667286 | http://www.w3.org/2000/01/rdf-schema#comment | "The invariant chain (Ii) prevents binding of ligands to major histocompatibility complex (MHC) class II molecules in the endoplasmic reticulum and during intracellular transport. Stepwise removal of the Ii in a trans-Golgi compartment renders MHC class II molecules accessible for peptide loading, with CLIP (class II-associated Ii peptides) as the final fragment to be released. Here we show that CLIP can be subdivided into distinct functional regions. The C-terminal segment (residues 92-105) of the CLIP-(81-105) fragment mediates inhibition of self- and antigenic peptide binding to HLA-DR2 molecules. In contrast, the N-terminal segment CLIP-(81-98) binds to the Staphylococcus aureus enterotoxin B contact site outside the peptide-binding groove on the alpha 1 domain and does not interfere with peptide binding. Its functional significance appears to lie in the contribution to CLIP removal: the dissociation of CLIP-(81-105) is characterized by a fast off-rate, which is accelerated at endosomal pH, whereas in the absence of the N-terminal CLIP-(81-91), the off-rate of C-terminal CLIP-(92-105) is slow and remains unaltered at low pH. Mechanistically, the N-terminal segment of CLIP seems to prevent tight interactions of CLIP side chains with specificity pockets in the peptide-binding groove that normally occurs during maturation of long-lived class II-peptide complexes."xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.92.18.8313"xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://purl.uniprot.org/core/author | "Kropshofer H."xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://purl.uniprot.org/core/author | "Vogt A.B."xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://purl.uniprot.org/core/author | "Hammerling G.J."xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7667286 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://purl.uniprot.org/core/pages | "8313-8317"xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://purl.uniprot.org/core/title | "Structural features of the invariant chain fragment CLIP controlling rapid release from HLA-DR molecules and inhibition of peptide binding."xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://purl.uniprot.org/core/volume | "92"xsd:string |
| http://purl.uniprot.org/citations/7667286 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7667286 |
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| http://purl.uniprot.org/uniprot/#_Q30154-mappedCitation-7667286 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/7667286 |
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| http://purl.uniprot.org/uniprot/#_P05538-mappedCitation-7667286 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/7667286 |