A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling.

@article{Jones1992ANT,
  title={A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling.},
  author={Peter Jones and Graham J. Moore and David. M. Waisman},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 20},
  pages={
          13993-7
        }
}
A synthetic nonapeptide, Val-Leu-Ile-Arg-Ile-Met-Val-Ser-Arg, corresponding to residues 286-294 of annexin-II tetramer (A-IIt), was shown to completely inhibit the Ca(2+)-dependent bundling of F-actin by this protein. The inhibitory effect of the nonapeptide required preincubation with F-actin and was reversed by the addition of excess A-IIt. Kinetic analysis suggested that the nonapeptide reduced the K(0.5) but not the Vmax of F-actin bundling. In contrast, addition of excess nonapeptide to A… CONTINUE READING

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