2fny
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2fny.gif|left|200px]]<br /><applet load="2fny" size=" | + | [[Image:2fny.gif|left|200px]]<br /><applet load="2fny" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fny, resolution 3.00Å" /> | caption="2fny, resolution 3.00Å" /> | ||
'''Homobelactosin C bound to the yeast 20S proteasome'''<br /> | '''Homobelactosin C bound to the yeast 20S proteasome'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Most class I MHC ligands are generated from the vast majority of cellular | + | 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== | ==About this Structure== | ||
| - | 2FNY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ESY as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 2FNY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ESY:'>ESY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNY OCA]. |
==Reference== | ==Reference== | ||
| Line 18: | Line 18: | ||
[[Category: beta sandwich structure flanked by helices]] | [[Category: beta sandwich structure flanked by helices]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:19 2008'' |
Revision as of 15:23, 21 February 2008
|
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 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 Thu Feb 21 17:23:19 2008
