1xqh

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[[Image:1xqh.jpg|left|200px]]<br /><applet load="1xqh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xqh.jpg|left|200px]]
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caption="1xqh, resolution 1.75&Aring;" />
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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'''<br />
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{{Structure
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|PDB= 1xqh |SIZE=350|CAPTION= <scene name='initialview01'>1xqh</scene>, resolution 1.75&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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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'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1XQH is a [[Protein complex]] structure of sequences 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=1XQH OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15525938 15525938]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15525938 15525938]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: set9-p53 complex]]
[[Category: set9-p53 complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:13:17 2008''

Revision as of 13:13, 20 March 2008

Image:1xqh.jpg


PDB ID 1xqh

Drag the structure with the mouse to rotate
, resolution 1.75Å
Ligands:
Activity: Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Coordinates: save as pdb, mmCIF, xml



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. 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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