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PDBsum entry 1mdy
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Transcription/DNA
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PDB id
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1mdy
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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 myod bhlh domain-Dna complex: perspectives on DNA recognition and implications for transcriptional activation.
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Authors
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P.C.Ma,
M.A.Rould,
H.Weintraub,
C.O.Pabo.
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Ref.
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Cell, 1994,
77,
451-459.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA complex
has been solved and refined at 2.8 A resolution. This structure proves that bHLH
and bHLH-leucine zipper (bHLH-ZIP) proteins are remarkably similar; it helps us
understand subtle differences in binding preferences for these proteins; and it
has surprising implications for our understanding of transcription.
Specifically, Ala-114 and Thr-115, which are required for positive control in
the myogenic proteins, are buried at the protein-DNA interface. These residues
are not available for direct protein-protein contacts, but they may determine
the conformation of Arg-111. Comparisons with Max suggest that the conformation
of this arginine, which is different in the two structures, may play an
important role in myogenic transcription.
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