1ro4: Difference between revisions

Revision as of 19:21, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ro4.png

Template:STRUCTURE 1ro4

RDC-derived models of the zinc ribbon domain of human general transcription factor TFIIB (zinc free structures)RDC-derived models of the zinc ribbon domain of human general transcription factor TFIIB (zinc free structures)

Template:ABSTRACT PUBMED 14641108

About this StructureAbout this Structure

1RO4 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Probing Zn2+-binding effects on the zinc-ribbon domain of human general transcription factor TFIIB., Ghosh M, Elsby LM, Mal TK, Gooding JM, Roberts SG, Ikura M, Biochem J. 2004 Mar 1;378(Pt 2):317-24. PMID:14641108

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1ro4|  PDB=1ro4  |  SCENE=  }}
-'''RDC-derived models of the zinc ribbon domain of human general transcription factor TFIIB (zinc free structures)'''
+===RDC-derived models of the zinc ribbon domain of human general transcription factor TFIIB (zinc free structures)===
-==Overview==
+<!--
-The general transcription factor, TFIIB, plays an important role in the assembly of the pre-initiation complex. The N-terminal domain (NTD) of TFIIB contains a zinc-ribbon motif, which is responsible for the recruitment of RNA polymerase II and TFIIF to the core promoter region. Although zinc-ribbon motif structures of eukaryotic and archaeal TFIIBs have been reported previously, the structural role of Zn2 binding to TFIIB remains to be determined. In the present paper, we report NMR and biochemical studies of human TFIIB NTD, which characterize the structure and dynamics of the TFIIB Zn2-binding domain in both Zn2-bound and -free states. The NMR data show that, whereas the backbone fold of NTD is pre-formed in the apo state, Zn2 binding reduces backbone mobility in the b-turn (Arg28-Gly30), induces enhanced structural rigidity of the charged-cluster domain in the central linker region of TFIIB and appends a positive surface charge within the Zn2-binding site. V8 protease-sensitivity assays of full-length TFIIB support the Zn2-dependent structural changes. These structural effects of Zn2 binding on TFIIB may have a critical role in interactions with its binding partners, such as the Rpb1 subunit of RNA polymerase II.
+The line below this paragraph, {{ABSTRACT_PUBMED_14641108}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14641108 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14641108}}
 ==About this Structure==
-RO4 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=1RO4 OCA].
+RO4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RO4 OCA].
 ==Reference==
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 [[Category: Rubredoxin knuckle]]
 [[Category: Zinc ribbon]]
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