2fny
From Proteopedia
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|PDB= 2fny |SIZE=350|CAPTION= <scene name='initialview01'>2fny</scene>, resolution 3.00Å | |PDB= 2fny |SIZE=350|CAPTION= <scene name='initialview01'>2fny</scene>, resolution 3.00Å | ||
|SITE= | |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> | + | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fny OCA], [http://www.ebi.ac.uk/pdbsum/2fny PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fny RCSB]</span> | ||
}} | }} | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Groll, M.]] | [[Category: Groll, M.]] | ||
| - | [[Category: ESY]] | ||
[[Category: beta sandwich structure flanked by helice]] | [[Category: beta sandwich structure flanked by helice]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:21 2008'' |
Revision as of 00:05, 31 March 2008
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| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Proteasome endopeptidase complex, with EC number 3.4.25.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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