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2fny

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{{STRUCTURE_2fny| PDB=2fny | SCENE= }}
{{STRUCTURE_2fny| PDB=2fny | SCENE= }}
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'''Homobelactosin C bound to the yeast 20S proteasome'''
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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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{{ABSTRACT_PUBMED_16537370}}
==About this Structure==
==About this Structure==
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[[Category: Groll, M.]]
[[Category: Groll, M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:44:33 2008''

Revision as of 01:44, 29 July 2008

Image:2fny.png

Template:STRUCTURE 2fny

Homobelactosin C bound to the yeast 20S proteasome

Template:ABSTRACT PUBMED 16537370

About this Structure

2FNY is a Protein complex structure of sequences from Saccharomyces cerevisiae. 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

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