1MDY

CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION

Summary for 1MDY

• Entry DOI: 10.2210/pdb1mdy/pdb
• Descriptor: DNA (5'-D(*TP*CP*AP*AP*CP*AP*GP*CP*TP*GP*TP*TP*GP*A)-3'), PROTEIN (MYOD BHLH DOMAIN), ... (4 entities in total)
• Functional Keywords: protein-dna complex, transcription-dna complex, transcription/dna
• Biological source: Mus musculus (house mouse); More
• Cellular location: Nucleus:
• Total number of polymer chains: 8
• Total formula weight: 46985.60

Authors

Ma, P.C.M.,Rould, M.A.,Weintraub, H.,Pabo, C.O. (deposition date: 1994-06-09, release date: 1994-08-31, Last modification date: 2024-02-14)

Primary citation

Ma, P.C.,Rould, M.A.,Weintraub, H.,Pabo, C.O.
Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation.
Cell(Cambridge,Mass.), 77:451-459, 1994

PubMed Abstract: 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.

PubMed: 8181063
DOI: 10.1016/0092-8674(94)90159-7

Experimental method

X-RAY DIFFRACTION (2.8 Å)