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Complete assignment of the 1 H NMR spectrum and secondary structure of the DNA binding domain of GAL4
Author(s) -
Gadhavi Paresh L.,
Raine Andrew R.C.,
Alefounder Peter R.,
Laue Ernest D.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80504-c
Subject(s) - zinc finger , dna binding domain , dna , hmg box , chemistry , xenopus , binding domain , dna binding protein , transcription factor , binding site , crystallography , b3 domain , lim domain , stereochemistry , biochemistry , gene
Complete 1 H 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 C 2 H 2 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.