Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites.

@article{Martik2004DifferentialSA,
  title={Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites.},
  author={Diana Martik and Celia Baitinger and Paul Modrich},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 27},
  pages={
          28402-10
        }
}
We have examined the permissible nucleotide occupancy states of human MutSalpha. The MSH2.MSH6 heterodimer binds 1 mol of ADP and 1 mol of adenosine 5'-O-(thiotriphosphate) (ATPgammaS), with a K(d) for each nucleotide of about 1 microm. Anisotropy measurements using BODIPY TR and BODIPY FL fluorescent derivatives of ADP and 5'-adenylyl-beta,gamma-imidodiphosphate (AMPPNP) also indicate an interaction stoichiometry of 1 mol of ADP and 1 mol of triphosphate analogue per MutSalpha heterodimer. Di… CONTINUE READING
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