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Article

Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: prediction and rational design.

Genes & development - 1 Jun 1993

Vinson C R, Hai T, Boyd S M

Abstract excerpt

We propose an interhelical salt bridge rule to explain the dimerization specificity between the two amphipathic alpha-helices in the leucine zipper structure. Using the bZIP class of DNA-binding proteins as a model system, we predicted and designed novel dimerization partners. We predicted that ATF4, a member of the ATF/CREB family of transcription factors, would preferentially form heterodimers with IGEBP1, a...

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Source

Identifiers

PMID: 8504929
DOI: 10.1101/gad.7.6.1047

Genes

EBP
ATF4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: prediction and rational design.PMID 8504929Read ↗

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Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization.Semantic proximity Read ↗

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Buried asparagines determine the dimerization specificities of leucine zipper mutants.Semantic proximity Read ↗

Basic leucine zipper transcription factor Hac1 binds DNA in two distinct modes as revealed by microfluidic analyses.Semantic proximity Read ↗

Mapping the dimerization specificity of bZIP transcription factors in bread wheatSemantic proximity Read ↗

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