1MDY

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

1MDY の概要

• エントリーDOI: 10.2210/pdb1mdy/pdb
• 分子名称: 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)
• 機能のキーワード: protein-dna complex, transcription-dna complex, transcription/dna
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Nucleus:
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 46985.60

構造登録者

Ma, P.C.M.,Rould, M.A.,Weintraub, H.,Pabo, C.O. (登録日: 1994-06-09, 公開日: 1994-08-31, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)