2fny
From Proteopedia
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(New page: 200px<br /><applet load="2fny" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fny, resolution 3.00Å" /> '''Homobelactosin C bou...)
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Revision as of 08:31, 21 November 2007
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Homobelactosin C bound to the yeast 20S proteasome
Overview
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.
About this Structure
2FNY is a Protein complex structure of sequences from Saccharomyces cerevisiae with ESY as ligand. Active as Proteasome endopeptidase complex, with EC number 3.4.25.1 Full crystallographic information is available from OCA.
Reference
Inhibitor-binding mode of homobelactosin C to proteasomes: new insights into class I MHC ligand generation., Groll M, Larionov OV, Huber R, de Meijere A, Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4576-9. Epub 2006 Mar 13. PMID:16537370
Page seeded by OCA on Wed Nov 21 10:38:56 2007
