1pdq: Difference between revisions

Revision as of 03:30, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pdq.png

Template:STRUCTURE 1pdq

Polycomb chromodomain complexed with the histone H3 tail containing trimethyllysine 27.Polycomb chromodomain complexed with the histone H3 tail containing trimethyllysine 27.

Template:ABSTRACT PUBMED 12897054

About this StructureAbout this Structure

1PDQ is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains., Fischle W, Wang Y, Jacobs SA, Kim Y, Allis CD, Khorasanizadeh S, Genes Dev. 2003 Aug 1;17(15):1870-81. PMID:12897054

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1pdq.gif|left|200px]]
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-'''Polycomb chromodomain complexed with the histone H3 tail containing trimethyllysine 27.'''
+===Polycomb chromodomain complexed with the histone H3 tail containing trimethyllysine 27.===
-==Overview==
+<!--
-On the histone H3 tail, Lys 9 and Lys 27 are both methylation sites associated with epigenetic repression, and reside within a highly related sequence motif ARKS. Here we show that the chromodomain proteins Polycomb (Pc) and HP1 (heterochromatin protein 1) are highly discriminatory for binding to these sites in vivo and in vitro. In Drosophila S2 cells, and on polytene chromosomes, methyl-Lys 27 and Pc are both excluded from areas that are enriched in methyl-Lys 9 and HP1. Swapping of the chromodomain regions of Pc and HP1 is sufficient for switching the nuclear localization patterns of these factors, indicating a role for their chromodomains in both target site binding and discrimination. To better understand the molecular basis for the selection of methyl-lysine binding sites, we solved the 1.8 A structure of the Pc chromodomain in complex with a H3 peptide bearing trimethyl-Lys 27, and compared it with our previously determined structure of the HP1 chromodomain in complex with a H3 peptide bearing trimethyl-Lys 9. The Pc chromodomain distinguishes its methylation target on the H3 tail via an extended recognition groove that binds five additional residues preceding the ARKS motif.
+The line below this paragraph, {{ABSTRACT_PUBMED_12897054}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12897054 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12897054}}
 ==About this Structure==
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 [[Category: Polycomb]]
 [[Category: Trimethyllysine]]
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