2gfa: Difference between revisions
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[[Image:2gfa.gif|left|200px]]<br /> | [[Image:2gfa.gif|left|200px]]<br /><applet load="2gfa" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2gfa, resolution 2.100Å" /> | caption="2gfa, resolution 2.100Å" /> | ||
'''double tudor domain complex structure'''<br /> | '''double tudor domain complex structure'''<br /> | ||
==Overview== | ==Overview== | ||
Biological responses to histone methylation critically depend on the | 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. | ||
==About this Structure== | ==About this Structure== | ||
2GFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2GFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2GFA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bedford, M | [[Category: Bedford, M T.]] | ||
[[Category: Fang, J.]] | [[Category: Fang, J.]] | ||
[[Category: Huang, Y.]] | [[Category: Huang, Y.]] | ||
[[Category: Xu, R | [[Category: Xu, R M.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
[[Category: double tudor domain]] | [[Category: double tudor domain]] | ||
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[[Category: tudor tandem]] | [[Category: tudor tandem]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:31:10 2008'' | ||
Revision as of 18:31, 21 February 2008
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double tudor domain complex structure
OverviewOverview
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.
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
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