1pue
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(New page: 200px<br /><applet load="1pue" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pue, resolution 2.100Å" /> '''PU.1 ETS DOMAIN-DNA...)
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Revision as of 22:00, 20 November 2007
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PU.1 ETS DOMAIN-DNA COMPLEX
Overview
The Ets family of transcription factors, of which there are now about 35, members regulate gene expression during growth and development. They share, a conserved domain of around 85 amino acids which binds as a monomer to, the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure, of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is, similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts, with a ten-base-pair region of duplex DNA which takes up a uniform curve, of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop, architecture. Four of amino acids that directly interact with the DNA are, highly conserved: two arginines from the recognition helix lying in the, major groove, one lysine from the 'wing' that binds upstream of the core, GGAA sequence, and another lysine, from the 'turn' of the, 'helix-turn-helix' motif, which binds downstream and on the opposite, strand.
About this Structure
1PUE is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex., Kodandapani R, Pio F, Ni CZ, Piccialli G, Klemsz M, McKercher S, Maki RA, Ely KR, Nature. 1996 Apr 4;380(6573):456-60. PMID:8602247
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