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1imj

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(New page: 200px<br /> <applet load="1imj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1imj, resolution 2.20&Aring;" /> '''CRYSTAL STRUCTURE O...)
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<applet load="1imj" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1imj, resolution 2.20&Aring;" />
caption="1imj, resolution 2.20&Aring;" />
'''CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)'''<br />
'''CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)'''<br />
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==About this Structure==
==About this Structure==
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1IMJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IMJ OCA].
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1IMJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMJ OCA].
==Reference==
==Reference==
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[[Category: ccg1 interactor]]
[[Category: ccg1 interactor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:31:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:02:31 2008''

Revision as of 14:02, 15 February 2008


1imj, resolution 2.20Å

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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.

About this Structure

1IMJ is a Single protein structure of sequence from Homo sapiens with as ligand. 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

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