An undecided coiled coil: the leucine zipper of Nek2 kinase exhibits atypical conformational exchange dynamics.

ABSTRACT: Leucine zippers are oligomerization domains used in a wide range of proteins. Their structure is based on a highly conserved heptad repeat sequence in which two key positions are occupied by leucines. The leucine zipper of the cell cycle-regulated Nek2 kinase is important for its dimerization and activation. However, the sequence of this leucine zipper is most unusual in that leucines occupy only one of the two hydrophobic positions. The other position, depending on the register of the heptad repeat, is occupied by either acidic or basic residues. Using NMR spectroscopy, we show that this leucine zipper exists in two conformations of almost equal population that exchange with a rate of 17 s(-1). We propose that the two conformations correspond to the two possible registers of the heptad re

SUBMITTER: Croasdale R 

PROVIDER: S-EPMC3149346 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature