We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2g6q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2g6q.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2g6q.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2g6q| PDB=2g6q | SCENE= }}
{{STRUCTURE_2g6q| PDB=2g6q | SCENE= }}
-
'''Crystal structure of ING2 PHD domain in complex with H3K4Me3 peptide'''
+
===Crystal structure of ING2 PHD domain in complex with H3K4Me3 peptide===
-
==Overview==
+
<!--
-
Covalent modifications of histone tails have a key role in regulating chromatin structure and controlling transcriptional activity. In eukaryotes, histone H3 trimethylated at lysine 4 (H3K4me3) is associated with active chromatin and gene expression. We recently found that plant homeodomain (PHD) finger of tumour suppressor ING2 (inhibitor of growth 2) binds H3K4me3 and represents a new family of modules that target this epigenetic mark. The molecular mechanism of H3K4me3 recognition, however, remains unknown. Here we report a 2.0 A resolution structure of the mouse ING2 PHD finger in complex with a histone H3 peptide trimethylated at lysine 4. The H3K4me3 tail is bound in an extended conformation in a deep and extensive binding site consisting of elements that are conserved among the ING family of proteins. The trimethylammonium group of Lys 4 is recognized by the aromatic side chains of Y215 and W238 residues, whereas the intermolecular hydrogen-bonding and complementary surface interactions, involving Ala 1, Arg 2, Thr 3 and Thr 6 of the peptide, account for the PHD finger's high specificity and affinity. Substitution of the binding site residues disrupts H3K4me3 interaction in vitro and impairs the ability of ING2 to induce apoptosis in vivo. Strong binding of other ING and YNG PHD fingers suggests that the recognition of H3K4me3 histone code is a general feature of the ING/YNG proteins. Elucidation of the mechanisms underlying this novel function of PHD fingers provides a basis for deciphering the role of the ING family of tumour suppressors in chromatin regulation and signalling.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16728977}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16728977 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16728977}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Zhao, R.]]
[[Category: Zhao, R.]]
[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:45:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:22:33 2008''

Revision as of 12:22, 27 July 2008

Image:2g6q.png

Template:STRUCTURE 2g6q

Crystal structure of ING2 PHD domain in complex with H3K4Me3 peptide

Template:ABSTRACT PUBMED 16728977

About this Structure

2G6Q is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2., Pena PV, Davrazou F, Shi X, Walter KL, Verkhusha VV, Gozani O, Zhao R, Kutateladze TG, Nature. 2006 Jul 6;442(7098):100-3. Epub 2006 May 21. PMID:16728977

Page seeded by OCA on Sun Jul 27 15:22:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2g6q"
Personal tools