2fny
From Proteopedia
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| - | [[Image:2fny.gif|left|200px]] | + | [[Image:2fny.gif|left|200px]] |
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| - | '''Homobelactosin C bound to the yeast 20S proteasome''' | + | {{Structure |
| + | |PDB= 2fny |SIZE=350|CAPTION= <scene name='initialview01'>2fny</scene>, resolution 3.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ESY:BENZYL N-[(BENZYLOXY)CARBONYL]-D-ALANYL-N~6~-[(2S,3S,4S)-3-FORMYL-2-HYDROXY-4-METHYLHEXANOYL]-L-LYSINATE'>ESY</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Homobelactosin C bound to the yeast 20S proteasome''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FNY is a [ | + | 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]. |
==Reference== | ==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:[http:// | + | 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] |
[[Category: Proteasome endopeptidase complex]] | [[Category: Proteasome endopeptidase complex]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: Groll, M.]] | [[Category: Groll, M.]] | ||
[[Category: ESY]] | [[Category: ESY]] | ||
| - | [[Category: beta sandwich structure flanked by | + | [[Category: beta sandwich structure flanked by helice]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:54:41 2008'' |
Revision as of 14:54, 20 March 2008
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| , resolution 3.00Å | |||||||
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| Ligands: | |||||||
| Activity: | Proteasome endopeptidase complex, with EC number 3.4.25.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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