1apl
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(New page: 200px<br /><applet load="1apl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1apl, resolution 2.700Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 08:54, 20 November 2007
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CRYSTAL STRUCTURE OF A MAT-ALPHA2 HOMEODOMAIN-OPERATOR COMPLEX SUGGESTS A GENERAL MODEL FOR HOMEODOMAIN-DNA INTERACTIONS
Overview
The MAT alpha 2 homeodomain regulates the expression of cell type-specific, genes in yeast. We have determined the 2.7 A resolution crystal structure, of the alpha 2 homeodomain bound to a biologically relevant DNA sequence., The DNA in this complex is contacted primarily by the third of three, alpha-helices, with additional contacts coming from an N-terminal arm., Comparison of the yeast alpha 2 and the Drosophila engrailed, homeodomain-DNA complexes shows that the protein fold is highly conserved, despite a 3-residue insertion in alpha 2 and only 27% sequence identity, between the two homeodomains. Moreover, the orientation of the recognition, helix on the DNA is also conserved. This docking arrangement is maintained, by side chain contacts with the DNA--primarily the sugar-phosphate, backbone--that are identical in alpha 2 and engrailed. Since these, residues are conserved among all homeodomains, we propose that the, contacts with the DNA are also conserved and suggest a general model for, homeodomain-DNA interactions.
About this Structure
1APL is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions., Wolberger C, Vershon AK, Liu B, Johnson AD, Pabo CO, Cell. 1991 Nov 1;67(3):517-28. PMID:1682054
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