1NKP

Crystal structure of Myc-Max recognizing DNA

1NKP の概要

• エントリーDOI: 10.2210/pdb1nkp/pdb
• 分子名称: 5'-D(*CP*GP*AP*GP*TP*AP*GP*CP*AP*CP*GP*TP*GP*CP*TP*AP*CP*TP*C)-3', Myc proto-oncogene protein, Max protein, ... (4 entities in total)
• 機能のキーワード: transcription, dna, bhlhz, oncogene, heterodimer, transcription-dna complex, transcription/dna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 63749.38

構造登録者

Nair, S.K.,Burley, S.K. (登録日: 2003-01-03, 公開日: 2003-02-04, 最終更新日: 2023-08-16)

主引用文献

Nair, S.K.,Burley, S.K.
X-ray structures of Myc-Max and Mad-Max recognizing DNA: Molecular bases of regulation by proto-oncogenic transcription factors
Cell(Cambridge,Mass.), 112:193-205, 2003

PubMed Abstract: X-ray structures of the basic/helix-loop-helix/leucine zipper (bHLHZ) domains of Myc-Max and Mad-Max heterodimers bound to their common DNA target (Enhancer or E box hexanucleotide, 5'-CACGTG-3') have been determined at 1.9 A and 2.0 A resolution, respectively. E box recognition by these two structurally similar transcription factor pairs determines whether a cell will divide and proliferate (Myc-Max) or differentiate and become quiescent (Mad-Max). Deregulation of Myc has been implicated in the development of many human cancers, including Burkitt's lymphoma, neuroblastomas, and small cell lung cancers. Both quasisymmetric heterodimers resemble the symmetric Max homodimer, albeit with marked structural differences in the coiled-coil leucine zipper regions that explain preferential homo- and heteromeric dimerization of these three evolutionarily related DNA-binding proteins. The Myc-Max heterodimer, but not its Mad-Max counterpart, dimerizes to form a bivalent heterotetramer, which explains how Myc can upregulate expression of genes with promoters bearing widely separated E boxes.

PubMed: 12553908
DOI: 10.1016/S0092-8674(02)01284-9

実験手法

X-RAY DIFFRACTION (1.8 Å)