First time at Proteopedia? Click on the green links, they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

Getting better: Proteopedia will be down this Sunday, 21 March 2010 between 9:00-10:00 Israeli time, for hardware upgrade.

2gf7

From Proteopedia

Jump to: navigation, search


2gf7, resolution 2.20Å ()
Ligands:
Gene: JMJD2A, JMJD2, KIAA0677 (Homo sapiens)
Domains: TUDOR
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Double tudor domain structure

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2GF7 is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Feb 17 15:18:20 2009

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools