2jng
From Proteopedia
(New page: 200px<br /> <applet load="2jng" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jng" /> '''Solution structure of the CUL7-CPH domain f...) |
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caption="2jng" /> | caption="2jng" /> | ||
'''Solution structure of the CUL7-CPH domain from Homo Sapiens; Northeast Structural Genomics Consortium target HT1.'''<br /> | '''Solution structure of the CUL7-CPH domain from Homo Sapiens; Northeast Structural Genomics Consortium target HT1.'''<br /> | ||
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==Overview== | ==Overview== | ||
Cul7 is a member of the Cullin Ring Ligase (CRL) family and is required, for normal mouse development and cellular proliferation. Recently, a, region of Cul7 that is highly conserved in the p-53 associated, Parkin-like cytoplasmic protein, PARC, was shown to bind p53 directly., Here we identify the CPH domain (conserved domain within Cul7, PARC and, HERC2 proteins) of both Cul7 and PARC as a p53 interaction domain using, size exclusion chromatography and NMR spectroscopy. We present the first, structure of the evolutionary conserved CPH domain and provide novel, insight into the Cul7-p53 interaction. The NMR structure of the Cul7-CPH, domain reveals a fold similar to peptide interaction modules such as the, SH3, Tudor and KOW domains. The p53 interaction surface of both Cul7 and, PARC CPH domains was mapped to a conserved surface distinct from the, analogous peptide binding regions of SH3, KOW and Tudor domains, suggesting a novel mode of interaction. The CPH domain interaction surface, of p53 resides in the tetramerization domain and is formed by residues, contributed by at least two subunits. | Cul7 is a member of the Cullin Ring Ligase (CRL) family and is required, for normal mouse development and cellular proliferation. Recently, a, region of Cul7 that is highly conserved in the p-53 associated, Parkin-like cytoplasmic protein, PARC, was shown to bind p53 directly., Here we identify the CPH domain (conserved domain within Cul7, PARC and, HERC2 proteins) of both Cul7 and PARC as a p53 interaction domain using, size exclusion chromatography and NMR spectroscopy. We present the first, structure of the evolutionary conserved CPH domain and provide novel, insight into the Cul7-p53 interaction. The NMR structure of the Cul7-CPH, domain reveals a fold similar to peptide interaction modules such as the, SH3, Tudor and KOW domains. The p53 interaction surface of both Cul7 and, PARC CPH domains was mapped to a conserved surface distinct from the, analogous peptide binding regions of SH3, KOW and Tudor domains, suggesting a novel mode of interaction. The CPH domain interaction surface, of p53 resides in the tetramerization domain and is formed by residues, contributed by at least two subunits. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: 3-M syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=609577 609577]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2JNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2JNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JNG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:19:00 2008'' |
Revision as of 13:19, 23 January 2008
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Solution structure of the CUL7-CPH domain from Homo Sapiens; Northeast Structural Genomics Consortium target HT1.
Overview
Cul7 is a member of the Cullin Ring Ligase (CRL) family and is required, for normal mouse development and cellular proliferation. Recently, a, region of Cul7 that is highly conserved in the p-53 associated, Parkin-like cytoplasmic protein, PARC, was shown to bind p53 directly., Here we identify the CPH domain (conserved domain within Cul7, PARC and, HERC2 proteins) of both Cul7 and PARC as a p53 interaction domain using, size exclusion chromatography and NMR spectroscopy. We present the first, structure of the evolutionary conserved CPH domain and provide novel, insight into the Cul7-p53 interaction. The NMR structure of the Cul7-CPH, domain reveals a fold similar to peptide interaction modules such as the, SH3, Tudor and KOW domains. The p53 interaction surface of both Cul7 and, PARC CPH domains was mapped to a conserved surface distinct from the, analogous peptide binding regions of SH3, KOW and Tudor domains, suggesting a novel mode of interaction. The CPH domain interaction surface, of p53 resides in the tetramerization domain and is formed by residues, contributed by at least two subunits.
About this Structure
2JNG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of P53., Kaustov L, Lukin J, Lemak A, Duan S, Ho M, Doherty R, Penn LZ, Arrowsmith CH, J Biol Chem. 2007 Feb 12;. PMID:17298945
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