ISSN:
1573-3904
Keywords:
coiled coil
;
dimerisation affinity
;
dimerisation specificity
;
Fos
;
Jun
;
leucine zipper
;
protein–protein interactions
;
superzipper peptides
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Dimerisation of leucine zippers results from the parallel association of α-helices to form a coiled coil. Coiled coils comprise a heptad repeat, denoted as (abcdefg)n, where residues at positions a and d are hydrophobic and constitute the core of the dimer interface. Charged amino acids at the e and g positions of the coiled coil are thought to be the major influence on dimerisation specificity through the formation of attractive and repulsive interhelical electrostatic interactions. However, the variability of a-position residues in leucine zipper transcription factors prompted us to investigate their influence on dimerisation specificity. We demonstrate that mutation of a single interfacial a-position Ala residue to either Val, Ile or Leu significantly alters the homo- and heterodimerisation specificities of the leucine zipper domain from the c-Jun transcription factor. These results illustrate the importance of a-position residues in controlling leucine zipper dimerisation specificity in addition to providing substantial contributions to dimer stability.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008997705549
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