1imj: Difference between revisions
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'''CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)''' | {{Structure | ||
|PDB= 1imj |SIZE=350|CAPTION= <scene name='initialview01'>1imj</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE HUMAN CCG1/TAFII250-INTERACTING FACTOR B (CIB)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IMJ is a [ | 1IMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMJ OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14672934 14672934] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ccg1 interactor]] | [[Category: ccg1 interactor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:19 2008'' | ||
Revision as of 09:52, 20 March 2008
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| 1imj, resolution 2.20Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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