Mutagenesis analysis of human SM22: characterization of actin binding.

@article{Fu2000MutagenesisAO,
  title={Mutagenesis analysis of human SM22: characterization of actin binding.},
  author={Yang-Xin Fu and H w Liu and Sean M Forsythe and Paul Kogut and John F. McConville and Andrew J Halayko and Blanca Camoretti-Mercado and Julian Solway},
  journal={Journal of applied physiology},
  year={2000},
  volume={89 5},
  pages={1985-90}
}
SM22 is a 201-amino acid actin-binding protein expressed at high levels in smooth muscle cells. It has structural homology to calponin, but how SM22 binds to actin remains unknown. We performed site-directed mutagenesis to generate a series of NH(2)-terminal histidine (His)-tagged mutants of human SM22 in Escherichia coli and used these to analyze the functional importance of potential actin binding domains. Purified full-length recombinant SM22 bound to actin in vitro, as demonstrated by… CONTINUE READING

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