1swi Citations

An engineered allosteric switch in leucine-zipper oligomerization.

Nat Struct Biol 3 510-5 (1996)
Cited: 63 times
EuropePMC logo PMID: 8646536

Abstract

Controversy remains about the role of core side-chain packing in specifying protein structure. To investigate the influence of core packing on the oligomeric structure of a coiled coil, we engineered a GCN4 leucine zipper mutant that switches from two to three strands upon binding the hydrophobic ligands cyclohexane and benzene. In solution these ligands increased the apparent thermal stability and the oligomerization order of the mutant leucine zipper. The crystal structure of the peptide-benzene complex shows a single benzene molecule bound at the engineered site in the core of the trimer. These results indicate that coiled coils are well-suited to function as molecular switches and emphasize that core packing is an important determinant of oligomerization specificity.

Reviews citing this publication (13)

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Articles citing this publication (50)

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Related citations provided by authors (3)

  1. Crystal Structure of an Isoleucine-Zipper Trimer. Harbury PB, Kim PS, Alber T Nature 371 80- (1994)
  2. A Switch between Two-, Three-, and Four-Stranded Coiled Coils in GCN4 Leucine Zipper Mutants. Harbury PB, Zhang T, Kim PS, Alber T Science 262 1401- (1993)
  3. X-Ray Structure of the GCN4 Leucine Zipper. O'Shea EK, Klemm JD, Kim PS, Alber T Science 254 539- (1991)