1HDD

CRYSTAL STRUCTURE OF AN ENGRAILED HOMEODOMAIN-DNA COMPLEX AT 2.8 ANGSTROMS RESOLUTION: A FRAMEWORK FOR UNDERSTANDING HOMEODOMAIN-DNA INTERACTIONS

Summary for 1HDD

• Entry DOI: 10.2210/pdb1hdd/pdb
• Descriptor: DNA (5'-D(*TP*TP*TP*TP*GP*CP*CP*AP*TP*GP*TP*AP*AP*TP*TP*AP*C P*CP*TP*AP*A)-3'), DNA (5'-D(*AP*TP*TP*AP*GP*GP*TP*AP*AP*TP*TP*AP*CP*AP*TP*GP*G P*CP*AP*AP*A)-3'), PROTEIN (ENGRAILED HOMEODOMAIN) (3 entities in total)
• Functional Keywords: protein-dna complex, double helix, transcription-dna complex, transcription/dna
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Nucleus : P02836
• Total number of polymer chains: 4
• Total formula weight: 27820.51

Authors

Kissinger, C.R.,Liu, B.,Martin-Blanco, E.,Kornberg, T.B.,Pabo, C.O. (deposition date: 1991-09-16, release date: 1992-01-15, Last modification date: 2024-05-22)

Primary citation

Kissinger, C.R.,Liu, B.S.,Martin-Blanco, E.,Kornberg, T.B.,Pabo, C.O.
Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions.
Cell(Cambridge,Mass.), 63:579-590, 1990

PubMed Abstract: 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.

PubMed: 1977522
DOI: 10.1016/0092-8674(90)90453-L

Experimental method

X-RAY DIFFRACTION (2.8 Å)