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2fny

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(New page: 200px<br /><applet load="2fny" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fny, resolution 3.00&Aring;" /> '''Homobelactosin C bou...)
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[[Image:2fny.gif|left|200px]]<br /><applet load="2fny" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fny.gif|left|200px]]<br /><applet load="2fny" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2fny, resolution 3.00&Aring;" />
caption="2fny, resolution 3.00&Aring;" />
'''Homobelactosin C bound to the yeast 20S proteasome'''<br />
'''Homobelactosin C bound to the yeast 20S proteasome'''<br />
==Overview==
==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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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FNY OCA].
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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==
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[[Category: beta sandwich structure flanked by helices]]
[[Category: beta sandwich structure flanked by helices]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:38:56 2007''
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''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


2fny, resolution 3.00Å

Drag the structure with the mouse to rotate

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

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