This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2dy8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2dy8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2dy8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2dy8| PDB=2dy8 | SCENE= }}
{{STRUCTURE_2dy8| PDB=2dy8 | SCENE= }}
-
'''Solution structure of the second chromodomain of yeast Chd1'''
+
===Solution structure of the second chromodomain of yeast Chd1===
-
==Overview==
+
<!--
-
Chromodomain from heterochromatin protein 1 and polycomb protein is known to be a lysine-methylated histone H3 tail-binding module. Chromo-helicase/ATPase DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin remodeling factor, containing two tandem chromodomains. In human CHD1, both chromodomains are essential for specific binding to a K4 methylated histone H3 (H3 MeK4) peptide and are found to bind cooperatively in the crystal structure. For the budding yeast homologue, Chd1, the second but not the first chromodomain was once reported to bind to an H3 MeK4 peptide. Here, we reveal that neither the second chromodomain nor a region containing tandem chromodomains from yeast Chd1 bind to any lysine-methylated or arginine-methylated histone peptides that we examined. In addition, we examined the structures of the chromodomains from Chd1 by NMR. Although the tertiary structure of the region containing tandem chromodomains could not be obtained, the secondary structure deduced from NMR is well conserved in the tertiary structures of the corresponding first and second chromodomains determined individually by NMR. Both chromodomains of Chd1 demonstrate a structure similar to that of the corresponding part of CHD1, consisting of a three-stranded beta-sheet followed by a C-terminal alpha-helix. However, an additional helix between the first and second beta-strands, which is found in both of the first chromodomains of Chd1 and CHD1, is positioned in an entirely different manner in Chd1 and CHD1. In human CHD1 this helix forms the peptide-binding site. The amino acid sequences of the chromodomains could be well aligned on the basis of these structures. The alignment showed that yeast Chd1 lacks several key functional residues, which are responsible for specific binding to a methylated lysine residue in other chromodomains. Chd1 is likely to have no binding affinity for any H3 MeK peptide, as found in other chromodomain proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17098252}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17098252 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17098252}}
==About this Structure==
==About this Structure==
-
2DY8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DY8 OCA].
+
2DY8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DY8 OCA].
==Reference==
==Reference==
Line 25: Line 29:
[[Category: Okuda, M.]]
[[Category: Okuda, M.]]
[[Category: Chromatin remodeling]]
[[Category: Chromatin remodeling]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:36:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:54:38 2008''

Revision as of 18:54, 27 July 2008

Image:2dy8.png

Template:STRUCTURE 2dy8

Solution structure of the second chromodomain of yeast Chd1

Template:ABSTRACT PUBMED 17098252

About this Structure

2DY8 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

Reference

Structural polymorphism of chromodomains in Chd1., Okuda M, Horikoshi M, Nishimura Y, J Mol Biol. 2007 Jan 26;365(4):1047-62. Epub 2006 Oct 14. PMID:17098252

Page seeded by OCA on Sun Jul 27 21:54:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dy8"
Personal tools