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Buried polar residues and structural specificity in the GCN4 leucine zipper.

Gonzalez L, Woolfson DN, Alber T
Nat Struct Biol 3 1011-8 (1996)
Related entries: 1zik, 1zim

Cited: 135 times
EuropePMC logo PMID: 8946854

Abstract

A conserved asparagine (Asn 16) buried in the interface of the GCN4 leucine zipper selectively favours the parallel, dimeric, coiled-coil structure. To test if other polar residues confer oligomerization specificity, the structural effects of Gln and Lys substitutions for Asn 16 were characterized. Like the wild-type peptide, the Asn 16Lys mutant formed exclusively dimers. In contrast, Gln 16, despite its chemical similarity to Asn, allowed the peptide to form both dimers and trimers. The Gln 16 side chain was accommodated by qualitatively different interactions in the dimer and trimer crystal structures. These findings demonstrate that the structural selectivity of polar residues results not only from the burial of polar atoms, but also depends on the complementarity of the side-chain stereochemistry with the surrounding structural environment.

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  1. An Engineered Allosteric Switch in Leucine-Zipper Oligomerization. Gonzalez Junior L, Plecs JJ, Alber T Nat. Struct. Biol. 3 510- (1996)
  2. Crystal Structure of an Isoleucine-Zipper Trimer. Harbury PB, Kim PS, Alber T Nature 371 80- (1994)
  3. 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)
  4. X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil. O'Shea EK, Klemm JD, Kim PS, Alber T Science 254 539- (1991)

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