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.


1zz1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zz1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zz1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zz1| PDB=1zz1 | SCENE= }}
{{STRUCTURE_1zz1| PDB=1zz1 | SCENE= }}
-
'''Crystal structure of a HDAC-like protein with SAHA bound'''
+
===Crystal structure of a HDAC-like protein with SAHA bound===
-
==Overview==
+
<!--
-
Histone deacetylases (HDACs) are among the most promising targets in cancer therapy. However, structural information greatly enhancing the design of HDAC inhibitors as novel chemotherapeutics has not been available on class 2 HDACs so far. Here we present the structure of the bacterial FB188 HDAH (histone deacetylase-like amidohydrolase from Bordetella/Alcaligenes strain FB188) that reveals high sequential and functional homology to human class 2 HDACs. FB188 HDAH is capable to remove the acetyl moiety from acetylated histones. Several HDAC-specific inhibitors, which have been shown to inhibit tumor activity in both pre-clinical models and in clinical trials, also inhibit FB188 HDAH. We have determined the crystal structure of FB188 HDAH at a resolution of 1.6 angstroms in complex with the reaction product acetate, as well as in complex with the inhibitors suberoylanilide hydroxamic acid (SAHA) and cyclopentyle-propionyle hydroxamic acid (CypX) at a resolution of 1.57 angstroms and 1.75 angstroms, respectively. FB188 HDAH exhibits the canonical fold of class 1 HDACs and contains a catalytic zinc ion. The highest structural diversity compared to class 1 enzymes is found in loop regions especially in the area around the entrance of the active site, indicating significant differences among the acetylated proteins binding to class 1 and 2 HDACs, respectively.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16242151}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16242151 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16242151}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Schwienhorst, A.]]
[[Category: Schwienhorst, A.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:15:30 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:48:30 2008''

Revision as of 02:48, 28 July 2008

Image:1zz1.png

Template:STRUCTURE 1zz1

Crystal structure of a HDAC-like protein with SAHA bound

Template:ABSTRACT PUBMED 16242151

About this Structure

1ZZ1 is a Single protein structure of sequence from Bordetella sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of a bacterial class 2 histone deacetylase homologue., Nielsen TK, Hildmann C, Dickmanns A, Schwienhorst A, Ficner R, J Mol Biol. 2005 Nov 18;354(1):107-20. Epub 2005 Oct 7. PMID:16242151

Page seeded by OCA on Mon Jul 28 05:48:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zz1"
Personal tools