2qqr
From Proteopedia
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| , resolution 1.80Å | |||||||
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| Sites: | , , , , and | ||||||
| Ligands: | , | ||||||
| Gene: | JMJD2A, JHDM3A, JMJD2, KIAA0677 (Homo sapiens) | ||||||
| Related: | 2QQS
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
JMJD2A hybrid tudor domains
Overview
The lysine demethylase JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences (H3K4me3 and H4K20me3) through its tudor domains. Here we show using X-ray crystallography and calorimetry that H3K4me3 and H4K20me3, which are recognized with similar affinities by JMJD2A, adopt radically different binding modes, to the extent that we were able to design single point mutations in JMJD2A that inhibited the recognition of H3K4me3 but not H4K20me3 and vice versa.
About this Structure
2QQR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor., Lee J, Thompson JR, Botuyan MV, Mer G, Nat Struct Mol Biol. 2008 Jan;15(1):109-11. Epub 2007 Dec 16. PMID:18084306
Page seeded by OCA on Mon Mar 31 04:52:19 2008
Categories: Homo sapiens | Single protein | Botuyan, M V. | Lee, J. | Mer, G. | Chromatin regulator | Dioxygenase | Histone lysine demethylase | Host-virus interaction | Iron | Metal binding protein | Metal-binding | Nucleus | Oxidoreductase | Phosphorylation | Polymorphism | Tandem hybrid tudor domain | Transcription | Transcription regulation | Zinc | Zinc-finger
