1hdd
From Proteopedia
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CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING HOMEODOMAIN-DNA INTERACTIONS
Overview
The crystal structure of a complex containing the engrailed homeodomain, and a duplex DNA site has been determined at 2.8 A resolution and refined, to a crystallographic R factor of 24.4%. In this complex, two separate, regions of the 61 amino acid polypeptide contact a TAAT subsite. An, N-terminal arm fits into the minor groove, and the side chains of Arg-3, and Arg-5 make contacts near the 5' end of this "core consensus" binding, site. An alpha helix fits into the major groove, and the side chains of, IIe-47 and Asn-51 contact base pairs near the 3' end of the TAAT site., This "recognition helix" is part of a structurally conserved, helix-turn-helix unit, but these helices are longer than the corresponding, helices in the lambda repressor, and the relationship between the, helix-turn-helix unit and the DNA is significantly different.
About this Structure
1HDD is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions., Kissinger CR, Liu BS, Martin-Blanco E, Kornberg TB, Pabo CO, Cell. 1990 Nov 2;63(3):579-90. PMID:1977522
Page seeded by OCA on Tue Nov 20 16:32:03 2007
