2pqw

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{{STRUCTURE_2pqw| PDB=2pqw | SCENE= }}
{{STRUCTURE_2pqw| PDB=2pqw | SCENE= }}
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'''Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form'''
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===Crystal structure of L3MBTL1 in complex with H4K20Me2 (residues 17-25), trigonal form===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 18026117 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18026117}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomics consortium]]
[[Category: Structural genomics consortium]]
[[Category: Transcription]]
[[Category: Transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:39:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:21:43 2008''

Revision as of 04:21, 29 July 2008

Image:2pqw.png

Template:STRUCTURE 2pqw

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

Template:ABSTRACT PUBMED 18026117

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

Page seeded by OCA on Tue Jul 29 07:21:43 2008

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