2gfa: Difference between revisions

Revision as of 04:06, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2gfa.png

Template:STRUCTURE 2gfa

double tudor domain complex structuredouble tudor domain complex structure

Template:ABSTRACT PUBMED 16601153

About this StructureAbout this Structure

2GFA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A., Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM, Science. 2006 May 5;312(5774):748-51. Epub 2006 Apr 6. PMID:16601153

Page seeded by OCA on Tue Jul 29 04:06:51 2008

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OCA

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-'''double tudor domain complex structure'''
+===double tudor domain complex structure===
-==Overview==
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-Biological responses to histone methylation critically depend on the faithful readout and transduction of the methyl-lysine signal by "effector" proteins, yet our understanding of methyl-lysine recognition has so far been limited to the study of histone binding by chromodomain and WD40-repeat proteins. The double tudor domain of JMJD2A, a Jmjc domain-containing histone demethylase, binds methylated histone H3-K4 and H4-K20. We found that the double tudor domain has an interdigitated structure, and the unusual fold is required for its ability to bind methylated histone tails. The cocrystal structure of the JMJD2A double tudor domain with a trimethylated H3-K4 peptide reveals that the trimethyl-K4 is bound in a cage of three aromatic residues, two of which are from the tudor-2 motif, whereas the binding specificity is determined by side-chain interactions involving amino acids from the tudor-1 motif. Our study provides mechanistic insights into recognition of methylated histone tails by tudor domains and reveals the structural intricacy of methyl-lysine recognition by two closely spaced effector domains.
+The line below this paragraph, {{ABSTRACT_PUBMED_16601153}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Trimethyl histone h3 lysine 4]]
 [[Category: Tudor tandem]]
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