2f4m: Difference between revisions

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[[Image:2f4m.gif|left|200px]]
{{Seed}}
[[Image:2f4m.png|left|200px]]


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{{STRUCTURE_2f4m|  PDB=2f4m  |  SCENE=  }}  
{{STRUCTURE_2f4m|  PDB=2f4m  |  SCENE=  }}  


'''The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs'''
===The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs===




==Overview==
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Peptide N-glycanase removes N-linked oligosaccharides from misfolded glycoproteins as part of the endoplasmic reticulum-associated degradation pathway. This process involves the formation of a tight complex of peptide N-glycanase with Rad23 in yeast and the orthologous HR23 proteins in mammals. In addition to its function in endoplasmic reticulum-associated degradation, HR23 is also involved in DNA repair, where it plays an important role in damage recognition in complex with the xeroderma pigmentosum group C protein. To characterize the dual role of HR23, we have determined the high resolution crystal structure of the mouse peptide N-glycanase catalytic core in complex with the xeroderma pigmentosum group C binding domain from HR23B. Peptide N-glycanase features a large cleft between its catalytic cysteine protease core and zinc binding domain. Opposite the zinc binding domain is the HR23B-interacting region, and surprisingly, the complex interface is fundamentally different from the orthologous yeast peptide N-glycanase-Rad23 complex. Different regions on both proteins are involved in complex formation, revealing an amazing degree of divergence in the interaction between two highly homologous proteins. Furthermore, the mouse peptide N-glycanase-HR23B complex mimics the interaction between xeroderma pigmentosum group C and HR23B, thereby providing a first structural model of how the two proteins interact within the nucleotide excision repair cascade in higher eukaryotes. The different interaction interfaces of the xeroderma pigmentosum group C binding domains in yeast and mammals suggest a co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways.
The line below this paragraph, {{ABSTRACT_PUBMED_16500903}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16500903}}


==About this Structure==
==About this Structure==
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[[Category: Transglutaminase]]
[[Category: Transglutaminase]]
[[Category: Ubiquitin-dependent protein degradation]]
[[Category: Ubiquitin-dependent protein degradation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:27:12 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:34:59 2008''

Revision as of 22:35, 28 July 2008

File:2f4m.png

Template:STRUCTURE 2f4m

The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs

Template:ABSTRACT PUBMED 16500903

About this Structure

2F4M is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways., Zhao G, Zhou X, Wang L, Li G, Kisker C, Lennarz WJ, Schindelin H, J Biol Chem. 2006 May 12;281(19):13751-61. Epub 2006 Feb 24. PMID:16500903

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