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| - | [[Image:2fny.gif|left|200px]] | + | #REDIRECT [[3e47]] This PDB entry is obsolete and replaced by 3e47 |
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| - | {{STRUCTURE_2fny| PDB=2fny | SCENE= }}
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| - | '''Homobelactosin C bound to the yeast 20S proteasome'''
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| - | ==Overview==
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| - | 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.
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| - | ==About this Structure==
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| - | 2FNY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNY OCA].
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| - | ==Reference==
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| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16537370 16537370]
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| - | [[Category: Proteasome endopeptidase complex]]
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| - | [[Category: Protein complex]]
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| - | [[Category: Saccharomyces cerevisiae]]
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| - | [[Category: Groll, M.]]
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| - | [[Category: Beta sandwich structure flanked by helice]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:07:01 2008''
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