CRYSTAL-STRUCTURE OF MYOD BHLH DOMAIN-DNA COMPLEX - PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION
CRYSTAL-STRUCTURE OF MYOD BHLH DOMAIN-DNA COMPLEX - PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION
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DOI：
10.1016/0092-8674(94)90159-7
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发表时间：
1994-05-06
期刊：
影响因子：
64.5
通讯作者：
PABOT, CO
中科院分区：
文献类型：
--
作者：
MA, PCM;ROULD, MA;PABOT, CO
在2.8埃分辨率下对MyoD碱性-螺旋-环-螺旋(BHLH)结构域-DNA复合体的晶体结构进行了求解和精化。这种结构证明了bHLH和bHLH-亮氨酸拉链(bHLH-ZIP)蛋白质非常相似；它帮助我们了解这些蛋白质结合偏好的细微差异；它对我们对转录的理解具有令人惊讶的意义。具体来说，ALA-114和Thr-115是肌源性蛋白中阳性控制所必需的，它们被埋在蛋白质-DNA界面上。这些残基不能与蛋白质直接接触，但它们可能决定Arg-111的构象。与Max的比较表明，这种在两种结构中不同的精氨酸的构象可能在生肌转录中发挥重要作用。
The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA complex has been solved and refined at 2.8 Angstrom 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.