1yrn
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(New page: 200px<br /><applet load="1yrn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yrn, resolution 2.500Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 04:53, 21 November 2007
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CRYSTAL STRUCTURE OF THE MATA1/MATALPHA2 HOMEODOMAIN HETERODIMER BOUND TO DNA
Overview
The Saccharomyces cerevisiae MATa1 and MAT alpha 2 homeodomain proteins, which play a role in determining yeast cell type, form a heterodimer that, binds DNA and represses transcription in a cell type-specific manner., Whereas the alpha 2 and a1 proteins on their own have only modest affinity, for DNA, the a1/alpha 2 heterodimer binds DNA with high specificity and, affinity. The three-dimensional crystal structure of the a1/alpha 2, homeodomain heterodimer bound to DNA was determined at a resolution of 2.5, A. The a1 and alpha 2 homeodomains bind in a head-to-tail orientation, with heterodimer contacts mediated by a 16-residue tail located, carboxyl-terminal to the alpha 2 homeodomain. This tail becomes ordered in, the presence of a1, part of it forming a short amphipathic helix that, packs against the a1 homeodomain between helices 1 and 2. A pronounced 60, degree bend is induced in the DNA, which makes possible protein-protein, and protein-DNA contacts that could not take place in a straight DNA, fragment. Complex formation mediated by flexible protein-recognition, peptides attached to stably folded DNA binding domains may prove to be a, general feature of the architecture of other classes of eukaryotic, transcriptional regulators.
About this Structure
1YRN is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA., Li T, Stark MR, Johnson AD, Wolberger C, Science. 1995 Oct 13;270(5234):262-9. PMID:7569974
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