COMPLETE ASSIGNMENT OF THE H-1-NMR SPECTRUM AND SECONDARY STRUCTURE OF THE DNA-BINDING DOMAIN OF GAL4

被引：22

作者：

GADHAVI, PL ^{[1
]}

RAINE, ARC ^{[1
]}

ALEFOUNDER, PR ^{[1
]}

LAUE, ED ^{[1
]}

机构：

[1] DEPT BIOCHEM, TENNIS COURT RD, CAMBRIDGE CB2 1QW, ENGLAND

来源：

FEBS LETTERS | 1990年 / 276卷 / 1-2期

关键词：

GAL4; 2D H-1 NMR; SEQUENCE-SPECIFIC RESONANCE ASSIGNMENT; SECONDARY STRUCTURE; DNA BINDING; ZINC FINGER;

D O I：

10.1016/0014-5793(90)80504-C

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：

Complete H-1 NMR resonance assignments are presented for the cysteine rich region of the DNA binding domain of the yeast transcriptional activator GAL4. The protein contains short helical regions between Asp-12 and Leu-19 and between Lys-30 and Trp-36. It is clearly distinct from the C2H2 class of zinc finger protein typified by the Xenopus laevis transcription factor (TF)IIIA. We also find that the first SP(X)(X) sequence, a recently proposed DNA binding motif (residues 41 to 44), appears to be tightly packed against the metal binding domain.

引用

页码：49 / 53

页数：5

共 25 条

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