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PDBsum entry 1apl
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DNA binding protein/DNA
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PDB id
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1apl
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a mat alpha 2 homeodomain-Operator complex suggests a general model for homeodomain-Dna interactions.
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Authors
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C.Wolberger,
A.K.Vershon,
B.Liu,
A.D.Johnson,
C.O.Pabo.
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Ref.
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Cell, 1991,
67,
517-528.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray diffraction studies of a mat alpha 2-Dna complex.
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Authors
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C.Wolberger,
C.O.Pabo,
A.K.Vershon,
A.D.Johnson.
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Ref.
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J Mol Biol, 1991,
217,
11-13.
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PubMed id
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