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

TitleComplete assignment of the 1H NMR spectrum and secondary structure of the DNA binding domain of GAL4.
Publication TypeJournal Article
Year of Publication1990
AuthorsGadhavi, PL, Raine, AR, Alefounder, PR, Laue, ED
JournalFEBS Lett
Volume276
Issue1-2
Pagination49-53
Date Published1990 Dec 10
ISSN0014-5793
KeywordsAmino Acid Sequence, Binding Sites, DNA-Binding Proteins, Fungal Proteins, Hydrogen, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Protein Conformation, Saccharomyces cerevisiae Proteins, Transcription Factors, Zinc Fingers
Abstract

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.

DOI10.1016/0014-5793(90)80504-c
Alternate JournalFEBS Lett.
Citation Key10.1016/0014-5793(90)80504-c
PubMed ID2265711