1f3u
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1f3u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3u, resolution 1.70Å" /> '''CRYSTAL STRUCTURE O...)
Next diff →
Revision as of 14:42, 12 November 2007
|
CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF
Overview
General transcription factor IIF (TFIIF) is required for transcription by, RNA polymerase II; it consists minimally of a heterodimer of RNA, polymerase-associated proteins RAP30 and RAP74. According to solution and, mutagenesis studies, the multiple domains of RAP30 and RAP74 bind PolII, TFIIB, TAF250 and DNA in interactions that are essential for transcription, initiation and elongation. The X-ray structure of the RAP30/RAP74, interaction domains at 1.7 A resolution reveals a novel "triple barrel", dimerization fold and suggests with mutant data that interactions with the, transcription apparatus are mediated not only by this tripartite, beta-barrel, but also via flexible loops and alpha and beta-structures, extending from it.
About this Structure
1F3U is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution., Gaiser F, Tan S, Richmond TJ, J Mol Biol. 2000 Oct 6;302(5):1119-27. PMID:11183778
Page seeded by OCA on Mon Nov 12 16:48:48 2007
