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rdf:type |
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lifeskim:mentions |
umls-concept:C0017349,
umls-concept:C0030956,
umls-concept:C0086168,
umls-concept:C0175722,
umls-concept:C0205263,
umls-concept:C0330390,
umls-concept:C0596448,
umls-concept:C1561603,
umls-concept:C1708715,
umls-concept:C2003941,
umls-concept:C2346689
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pubmed:issue |
1
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pubmed:dateCreated |
1995-8-17
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pubmed:abstractText |
Human leukocyte antigen DM (HLA-DM) molecules are structurally related to classical MHC class II molecules and reside in the lysosome-like compartment where class II-restricted antigen processing is thought to occur. Mutant cell lines lacking HLA-DM are defective in antigen processing and accumulate class II molecules associated with a nested set of invariant chain-derived peptides (class II-associated invariant chain peptides, CLIP). Here we show that HLA-DM catalyzes the dissociation of CLIP from MHC class II-CLIP complexes in vitro and facilitates the binding of antigenic peptides. The reaction has an acidic pH optimum, consistent with its occurrence in a lysosome-like compartment in vivo. Antibody blocking experiments suggest that a transient interaction between HLA-DM and the MHC class II-CLIP complex is required.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/H2-M antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-D Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DM antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DR3 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Porins,
http://linkedlifedata.com/resource/pubmed/chemical/invariant chain,
http://linkedlifedata.com/resource/pubmed/chemical/omp1 protein, Chlamydia trachomatis
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
82
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
155-65
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:7606781-Amino Acid Sequence,
pubmed-meshheading:7606781-Animals,
pubmed-meshheading:7606781-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:7606781-Bacterial Outer Membrane Proteins,
pubmed-meshheading:7606781-Chlamydia trachomatis,
pubmed-meshheading:7606781-HLA-D Antigens,
pubmed-meshheading:7606781-HLA-DR3 Antigen,
pubmed-meshheading:7606781-Histocompatibility Antigens Class II,
pubmed-meshheading:7606781-Humans,
pubmed-meshheading:7606781-Hybrid Cells,
pubmed-meshheading:7606781-Hydrogen-Ion Concentration,
pubmed-meshheading:7606781-Mice,
pubmed-meshheading:7606781-Molecular Sequence Data,
pubmed-meshheading:7606781-Peptides,
pubmed-meshheading:7606781-Porins,
pubmed-meshheading:7606781-T-Lymphocytes
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pubmed:year |
1995
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pubmed:articleTitle |
HLA-DM induces CLIP dissociation from MHC class II alpha beta dimers and facilitates peptide loading.
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pubmed:affiliation |
Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510-8011, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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