Complete assignment of the 1H NMR spectrum and secondary structure of the DNA binding domain of GAL4

FEBS Letters

Alefounder, Peter R.¹  Laue, Ernest D.¹  Raine, Andrew R.C.¹  Gadhavi, Paresh L.¹ 

[1] Department of Biochemistry, Tennis Court Road, Cambridge, CB2 1QW, UK

关键词: GAL4;    2D 1H NMR;    Sequence-specific resonance assignment;    Secondary structure;    DNA binding;    Zinc finger;   

DOI  :  10.1016/0014-5793(90)80504-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Complete ¹H 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.

【 授权许可】

Unknown