1xqh
From Proteopedia
(New page: 200px<br /> <applet load="1xqh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xqh, resolution 1.75Å" /> '''Crystal structure o...) |
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caption="1xqh, resolution 1.75Å" /> | caption="1xqh, resolution 1.75Å" /> | ||
'''Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH'''<br /> | '''Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XQH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SAH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] Full crystallographic information is available from [http:// | + | 1XQH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: set9-p53 complex]] | [[Category: set9-p53 complex]] | ||
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Revision as of 15:10, 15 February 2008
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Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH
Contents |
Overview
p53 is a tumour suppressor that regulates the cellular response to, genotoxic stresses. p53 is a short-lived protein and its activity is, regulated mostly by stabilization via different post-translational, modifications. Here we report a novel mechanism of p53 regulation through, lysine methylation by Set9 methyltransferase. Set9 specifically methylates, p53 at one residue within the carboxyl-terminus regulatory region., Methylated p53 is restricted to the nucleus and the modification, positively affects its stability. Set9 regulates the expression of p53, target genes in a manner dependent on the p53-methylation site. The, crystal structure of a ternary complex of Set9 with a p53 peptide and the, cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecular, basis for recognition of p53 by this lysine methyltransferase.
Disease
Known diseases associated with this structure: Adrenal cortical carcinoma OMIM:[191170], Breast cancer OMIM:[191170], Colorectal cancer OMIM:[191170], Hepatocellular carcinoma OMIM:[191170], Histiocytoma OMIM:[191170], Li-Fraumeni syndrome OMIM:[191170], Multiple malignancy syndrome OMIM:[191170], Nasopharyngeal carcinoma OMIM:[191170], Osteosarcoma OMIM:[191170], Pancreatic cancer OMIM:[191170], Thyroid carcinoma OMIM:[191170]
About this Structure
1XQH is a Protein complex structure of sequences from Homo sapiens with as ligand. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Full crystallographic information is available from OCA.
Reference
Regulation of p53 activity through lysine methylation., Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D, Nature. 2004 Nov 18;432(7015):353-60. Epub 2004 Nov 3. PMID:15525938
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Categories: Histone-lysine N-methyltransferase | Homo sapiens | Protein complex | Barlev, N.A. | Chuikov, S. | Gamblin, S.J. | Ivanov, G.S. | Justin, N. | Kurash, J.K. | McKinney, K. | Prives, C. | Reinberg, D. | Tempst, P. | Wilson, J.R. | Xiao, B. | SAH | Lysine methylation | Set-domain | Set9-p53 complex
