TRANSCRIPTION FACTOR STRUCTURE AND DNA-BINDING

被引：26

作者：

WOLBERGER, C ^{[1
]}

机构：

[1] JOHNS HOPKINS UNIV, SCH MED, BALTIMORE, MD 21205 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1993年 / 3卷 / 01期

关键词：

D O I：

10.1016/0959-440X(93)90194-P

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Within the past year, structures have been determined for five transcription factors, each of which is a member of a different structural class. Papilloma virus E2 and the TFIID TATA-binding protein represent novel and unanticipated DNA-binding motifs. The GAL4 protein is a new kind of metal-binding domain, GCN4 is a basic-region leucine zipper protein, and MATalpha2 is a member of the homeodomain family. With the exception of TFIID, the structures of the DNA-bound protein have been determined, revealing how each of the folds is used to recognize specific DNA sequences.

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页码：3 / 10

页数：8

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