|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
12
|
|
pubmed:dateCreated |
2006-3-22
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Most class I MHC ligands are generated from the vast majority of cellular proteins by proteolysis within the ubiquitin-proteasome pathway and are presented on the cell surface by MHC class I molecules. Here, we present the crystallographic analysis of yeast 20S proteasome in complex with the inhibitor homobelactosin C. The structure reveals a unique inhibitor-binding mode and provides information about the composition of proteasomal primed substrate-binding sites. IFN-gamma inducible substitution of proteasomal constitutive subunits by immunosubunits modulates characteristics of generated peptides, thus producing fragments with higher preference for binding to MHC class I molecules. The structural data for the proteasome:homobelactosin C complex provide an explanation for involvement of immunosubunits in antigen generation and open perspectives for rational design of ligands, inhibiting exclusively constitutive proteasomes or immunoproteasomes.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-10500111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-10631934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-10724015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-12714773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-14698035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-15200308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-15571807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-15678420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-16275340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-1922384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-2017257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-5682314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-7477383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-7513522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-7583150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-7725097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-8066463,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-8113682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-8120905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-8206875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-8371781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-8389422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-8396732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-8431436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-9087403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-9312134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-9642094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16537370-9668046
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
21
|
|
pubmed:volume |
103
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
4576-9
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:16537370-Amino Acid Sequence,
pubmed-meshheading:16537370-Crystallography, X-Ray,
pubmed-meshheading:16537370-Cysteine Proteinase Inhibitors,
pubmed-meshheading:16537370-Histocompatibility Antigens Class I,
pubmed-meshheading:16537370-Ligands,
pubmed-meshheading:16537370-Molecular Sequence Data,
pubmed-meshheading:16537370-Peptides,
pubmed-meshheading:16537370-Proteasome Endopeptidase Complex,
pubmed-meshheading:16537370-Protein Subunits,
pubmed-meshheading:16537370-Saccharomyces cerevisiae
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation.
|
|
pubmed:affiliation |
Ludwig Maximilians Universität, Adolf Butenandt Institut, Butenandtstrasse 5, Gebäude B, D-81377 Munich, Germany. mgroll@med.uni-muenchen.de
|
|
pubmed:publicationType |
Journal Article
|
