Ferguson ZNF Sandbox: Difference between revisions

Two mutants in the N-terminal domain of ADR1, a yeast transcription factor that contains two Cys2-His2 zinc finger sequences spanning residues 102-159 were studied at the Department of Biochemistry at the University of Washington<ref>Hoffman, R.C.; Horvath, S.J.; Klevit, R.E. Structures of DNA-binding mutant zinc finger domains: implications for DNA binding. Protein Sci. 1993 June; 2(6): 951–965.</ref>. There are two point mutants at position 118 in the N-terminal zinc finger (ADR1b: 102-130) that adversely affect the DNA-binding activity of ADR1 that been identified: H118A and H118Y. Comparisons of wild-type ADR1b and the two mutants revealed that neither mutation causes a significant structural perturbation. The structures indicate that the DNA binding properties of the His 118 mutants are dependent on the identity of the side chain at position 118, which makes a direct DNA contact in the wild-type ADR1 protein. The results suggest that the identity of the side chain at the middle DNA contact position in Cys2-His2 zinc fingers may be changed regarding the domain structure and this change can and will affect the affinity of the protein-DNA interaction<ref>Hoffman, R.C.; Horvath, S.J.; Klevit, R.E. Structures of DNA-binding mutant zinc finger domains: implications for DNA binding. Protein Sci. 1993 June; 2(6): 951–965.</ref>.