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Article

Fos leucine zipper variants with increased association capacity.

The Journal of biological chemistry - 29 Sept 1995

Porte D, Oertel-Buchheit P, Granger-Schnarr M, Schnarr M

Abstract excerpt

The Fos wild-type leucine zipper is unable to support homodimerization. This finding is generally explained by the negative net charge of the Fos zipper leading to the electrostatic repulsion of two monomers. Using a LexA-dependent in vivo assay in Escherichia coli, we show here that additional antideterminants for Fos zipper association are the residues in position a within the Fos zipper interface. If the...

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Identifiers

PMID: 7559397
DOI: 10.1074/jbc.270.39.22721

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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.

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Fos leucine zipper variants with increased association capacity.PMID 7559397Read ↗

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