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Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: A framework for understanding homeodomain-DNA interactions
Open accessAbstract
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.
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Metadata
- Authors
- Kissinger, C. R., Liu, B., Martin-Blanco, E., Kornberg, T. B., & Pabo, C. O.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1990-11
- Volume
- 63
- Issue
- 3
- Pages
- 579-590
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2076849893
- Cited by
- 986
- References
- 0
- FWCI
- 34.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
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