2pqw

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|PDB= 2pqw |SIZE=350|CAPTION= <scene name='initialview01'>2pqw</scene>, resolution 2.00&Aring;
|PDB= 2pqw |SIZE=350|CAPTION= <scene name='initialview01'>2pqw</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>
|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])
 +
|DOMAIN=
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|RELATEDENTRY=[[2rjc|2RJC]], [[2rjd|2RJD]], [[2rje|2RJE]], [[2rjf|2RJF]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqw OCA], [http://www.ebi.ac.uk/pdbsum/2pqw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pqw RCSB]</span>
}}
}}
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[[Category: Vedadi, M.]]
[[Category: Vedadi, M.]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J.]]
-
[[Category: ACT]]
 
[[Category: l(3)mbt-like protein]]
[[Category: l(3)mbt-like protein]]
[[Category: sgc]]
[[Category: sgc]]
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[[Category: transcription]]
[[Category: transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:39:34 2008''

Revision as of 01:39, 31 March 2008

Image:2pqw.jpg


PDB ID 2pqw

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: ,
Gene: L3MBTL, KIAA0681, L3MBT (Homo sapiens)
Related: 2RJC, 2RJD, 2RJE, 2RJF


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



Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form


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

2PQW 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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