2rjd

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|ACTIVITY=
|ACTIVITY=
|GENE= L3MBTL, KIAA0681, L3MBT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= L3MBTL, KIAA0681, L3MBT ([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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|RELATEDENTRY=[[2pqw|2PQW]], [[2rjc|2RJC]], [[2rje|2RJE]], [[2rjf|2RJF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjd OCA], [http://www.ebi.ac.uk/pdbsum/2rjd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rjd RCSB]</span>
}}
}}
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:36:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:01:09 2008''

Revision as of 02:01, 31 March 2008

Image:2rjd.gif


PDB ID 2rjd

Drag the structure with the mouse to rotate
, resolution 1.65Å
Gene: L3MBTL, KIAA0681, L3MBT (Homo sapiens)
Related: 2PQW, 2RJC, 2RJE, 2RJF


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of L3MBTL1 protein


Overview

Crystal structures of the L3MBTL1 MBT repeats in complex with histone H4 peptides dimethylated on Lys20 (H4K20me2) show that only the second of the three MBT repeats can bind mono- and dimethylated histone peptides. Its binding pocket has similarities to that of 53BP1 and is able to recognize the degree of histone lysine methylation. An unexpected mode of peptide-mediated dimerization suggests a possible mechanism for chromatin compaction by L3MBTL1.

About this Structure

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

Reference

L3MBTL1 recognition of mono- and dimethylated histones., Min J, Allali-Hassani A, Nady N, Qi C, Ouyang H, Liu Y, MacKenzie F, Vedadi M, Arrowsmith CH, Nat Struct Mol Biol. 2007 Dec;14(12):1229-30. Epub 2007 Nov 18. PMID:18026117

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