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.

1imj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1imj.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1imj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1imj| PDB=1imj | SCENE= }}
{{STRUCTURE_1imj| PDB=1imj | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)'''
+
===CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)===
-
==Overview==
+
<!--
-
The general transcription initiation factor TFIID and its interactors play critical roles in regulating the transcription from both naked and chromatin DNA. We have isolated a novel TFIID interactor that we denoted as CCG1/TAF(II)250-interacting factor B (CIB). We show here that CIB activates transcription. To further understand the function of this protein, we determined its crystal structure at 2.2-Angstroms resolution. The tertiary structure of CIB reveals an alpha/beta-hydrolase fold that resembles structures in the prokaryotic alpha/beta-hydrolase family proteins. It is not similar in structure or primary sequence to any eukaryotic transcription or chromatin factors that have been reported to date. CIB possesses a conserved catalytic triad that is found in other alpha/beta-hydrolases, and our in vitro studies confirmed that it bears hydrolase activity. However, CIB differs from other alpha/beta-hydrolases in that it lacks a binding site excursion, which facilitates the substrate selectivity of the other alpha/beta-hydrolases. Further functional characterization of CIB based on its tertiary structure and through biochemical studies may provide novel insights into the mechanisms that regulate eukaryotic transcription.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14672934}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14672934 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14672934}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Alpha/beta hydrolase]]
[[Category: Alpha/beta hydrolase]]
[[Category: Ccg1 interactor]]
[[Category: Ccg1 interactor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:09:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:32:51 2008''

Revision as of 10:32, 1 July 2008

Image:1imj.png

Template:STRUCTURE 1imj

CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)

Template:ABSTRACT PUBMED 14672934

About this Structure

1IMJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of CCG1/TAF(II)250-interacting factor B (CIB)., Padmanabhan B, Kuzuhara T, Adachi N, Horikoshi M, J Biol Chem. 2004 Mar 5;279(10):9615-24. Epub 2003 Dec 11. PMID:14672934

Page seeded by OCA on Tue Jul 1 13:32:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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