3b7b

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[[Image:3b7b.jpg|left|200px]]
[[Image:3b7b.jpg|left|200px]]
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{{Structure
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|PDB= 3b7b |SIZE=350|CAPTION= <scene name='initialview01'>3b7b</scene>, resolution 2.99&Aring;
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The line below this paragraph, containing "STRUCTURE_3b7b", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+5'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+6'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+7'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+A+8'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+B+1'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+B+2'>AC6</scene>, <scene name='pdbsite=AC7:So4+Binding+Site+For+Residue+B+3'>AC7</scene> and <scene name='pdbsite=AC8:So4+Binding+Site+For+Residue+B+4'>AC8</scene>
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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=SO4:SULFATE+ION'>SO4</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= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= EHMT1, EUHMTASE1, KIAA1876 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_3b7b| PDB=3b7b | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b7b OCA], [http://www.ebi.ac.uk/pdbsum/3b7b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b7b RCSB]</span>
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}}
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'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)'''
'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)'''
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[[Category: Collins, R E.]]
[[Category: Collins, R E.]]
[[Category: Horton, J R.]]
[[Category: Horton, J R.]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: ank repeat]]
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[[Category: Ank repeat]]
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[[Category: ankyrin repeat]]
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[[Category: Ankyrin repeat]]
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[[Category: chromatin regulator]]
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[[Category: Chromatin regulator]]
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[[Category: methyltransferase]]
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[[Category: Methyltransferase]]
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[[Category: nucleus]]
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[[Category: Nucleus]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: polymorphism]]
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[[Category: Polymorphism]]
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[[Category: s-adenosyl-l-methionine]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:28:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:23:42 2008''
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Revision as of 17:28, 4 May 2008

Image:3b7b.jpg

Template:STRUCTURE 3b7b

EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)


Overview

Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.

About this Structure

3B7B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules., Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X, Nat Struct Mol Biol. 2008 Mar;15(3):245-50. Epub 2008 Feb 10. PMID:18264113 Page seeded by OCA on Sun May 4 20:28:07 2008

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