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.


2h8n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2h8n.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2h8n.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2h8n| PDB=2h8n | SCENE= }}
{{STRUCTURE_2h8n| PDB=2h8n | SCENE= }}
-
'''Structure of a glutamine-rich domain from histone deacetylase 4'''
+
===Structure of a glutamine-rich domain from histone deacetylase 4===
-
==Overview==
+
<!--
-
Glutamine-rich sequences exist in a wide range of proteins across multiple species. A subset of glutamine-rich sequences has been shown to form amyloid fibers implicated in human diseases. The physiological functions of these sequence motifs are not well understood, partly because of the lack of structural information. Here we have determined a high-resolution structure of a glutamine-rich domain from human histone deacetylase 4 (HDAC4) by x-ray crystallography. The glutamine-rich domain of HDAC4 (19 glutamines of 68 residues) folds into a straight alpha-helix that assembles as a tetramer. In contrast to most coiled coil proteins, the HDAC4 tetramer lacks regularly arranged apolar residues and an extended hydrophobic core. Instead, the protein interfaces consist of multiple hydrophobic patches interspersed with polar interaction networks, wherein clusters of glutamines engage in extensive intra- and interhelical interactions. In solution, the HDAC4 tetramer undergoes rapid equilibrium with monomer and intermediate species. Structure-guided mutations that expand or disrupt hydrophobic patches drive the equilibrium toward the tetramer or monomer, respectively. We propose that a general role of glutamine-rich motifs be to mediate protein-protein interactions characteristic of a large component of polar interaction networks that may facilitate reversible assembly and disassembly of protein complexes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17360518}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17360518 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17360518}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Alpha helix]]
[[Category: Alpha helix]]
[[Category: Polar zipper]]
[[Category: Polar zipper]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:59:50 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:14:51 2008''

Revision as of 05:14, 29 July 2008

Image:2h8n.png

Template:STRUCTURE 2h8n

Structure of a glutamine-rich domain from histone deacetylase 4

Template:ABSTRACT PUBMED 17360518

About this Structure

2H8N is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains., Guo L, Han A, Bates DL, Cao J, Chen L, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4297-302. Epub 2007 Mar 5. PMID:17360518

Page seeded by OCA on Tue Jul 29 08:14:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h8n"
Personal tools