1vkg

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[[Image:1vkg.jpg|left|200px]]
[[Image:1vkg.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1vkg |SIZE=350|CAPTION= <scene name='initialview01'>1vkg</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_1vkg", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CRI:5-(4-METHYL-BENZOYLAMINO)-BIPHENYL-3,4&#39;-DICARBOXYLIC+ACID+3-DIMETHYLAMIDE-4&#39;-HYDROXYAMIDE'>CRI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= HDAC8, HDACL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1vkg| PDB=1vkg | SCENE= }}
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|RELATEDENTRY=[[1t64|1T64]], [[1t67|1T67]], [[1t69|1T69]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vkg OCA], [http://www.ebi.ac.uk/pdbsum/1vkg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vkg RCSB]</span>
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}}
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'''Crystal Structure of Human HDAC8 complexed with CRA-19156'''
'''Crystal Structure of Human HDAC8 complexed with CRA-19156'''
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[[Category: Verner, E.]]
[[Category: Verner, E.]]
[[Category: Wynands, R.]]
[[Category: Wynands, R.]]
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[[Category: histone deacetylase]]
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[[Category: Histone deacetylase]]
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[[Category: zinc hydrolase]]
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[[Category: Zinc hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:38:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:25:40 2008''
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Revision as of 09:38, 3 May 2008

Image:1vkg.jpg

Template:STRUCTURE 1vkg

Crystal Structure of Human HDAC8 complexed with CRA-19156


Overview

Modulation of the acetylation state of histones plays a pivotal role in the regulation of gene expression. Histone deacetylases (HDACs) catalyze the removal of acetyl groups from lysines near the N termini of histones. This reaction promotes the condensation of chromatin, leading to repression of transcription. HDAC deregulation has been linked to several types of cancer, suggesting a potential use for HDAC inhibitors in oncology. Here we describe the first crystal structures of a human HDAC: the structures of human HDAC8 complexed with four structurally diverse hydroxamate inhibitors. This work sheds light on the catalytic mechanism of the HDACs, and on differences in substrate specificity across the HDAC family. The structure also suggests how phosphorylation of Ser39 affects HDAC8 activity.

About this Structure

1VKG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases., Somoza JR, Skene RJ, Katz BA, Mol C, Ho JD, Jennings AJ, Luong C, Arvai A, Buggy JJ, Chi E, Tang J, Sang BC, Verner E, Wynands R, Leahy EM, Dougan DR, Snell G, Navre M, Knuth MW, Swanson RV, McRee DE, Tari LW, Structure. 2004 Jul;12(7):1325-34. PMID:15242608 Page seeded by OCA on Sat May 3 12:38:34 2008

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OCA

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