Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract

The bZIP motif is characterized by a leucine zipper domain that mediates dimerization and a basic domain that contacts DNA. A series of transition metal dimerization domains were used to alter systematically the relative orientation of basic domain peptides. Both the affinity and the specificity of the peptide-DNA interaction depend on domain orientation. These results indicate that the precise configuration linking the domains is important; dimerization is not always sufficient for DNA binding. This approach to studying the effect of orientation on protein function complements mutagenesis and could be used in many systems.

Bibliography

Cuenoud, B., & Schepartz, A. (1993). Altered Specificity of DNA-Binding Proteins with Transition Metal Dimerization Domains. Science, 259(5094), 510–513.

Authors 2
  1. Bernard Cuenoud (first)
  2. Alanna Schepartz (additional)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 5, 2006, 7:05 p.m.)
Deposited 1 year, 7 months ago (Jan. 15, 2024, 5:19 a.m.)
Indexed 3 months ago (June 5, 2025, 7:47 a.m.)
Issued 32 years, 7 months ago (Jan. 22, 1993)
Published 32 years, 7 months ago (Jan. 22, 1993)
Published Print 32 years, 7 months ago (Jan. 22, 1993)
Funders 0

None

@article{Cuenoud_1993, title={Altered Specificity of DNA-Binding Proteins with Transition Metal Dimerization Domains}, volume={259}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.8424173}, DOI={10.1126/science.8424173}, number={5094}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Cuenoud, Bernard and Schepartz, Alanna}, year={1993}, month=jan, pages={510–513} }