Evidence for a direct interaction between the penultimate aspartic acid of cholecystokinin and histidine 207, located in the second extracellular loop of the cholecystokinin B receptor.

@article{SilventePoirot1999EvidenceFA,
  title={Evidence for a direct interaction between the penultimate aspartic acid of cholecystokinin and histidine 207, located in the second extracellular loop of the cholecystokinin B receptor.},
  author={Sandrine Silvente-Poirot and Chantal Escrieut and C{\'e}line Gal{\'e}s and Jean Alain Fehrentz and Achim Escherich and Stephen Wank and Jean Mart{\'i}nez and Luis Moroder and Bernard Maigret and Mich{\`e}le Bouisson and Nicole Vaysse and Daniel Fourmy},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 33},
  pages={23191-7}
}
Recently, we reported that the mutation of His(207) to Phe located in the second extracellular loop of the cholecystokinin B receptor strongly affected cholecystokinin (CCK) binding (Silvente-Poirot, S., Escrieut, C., and Wank, S. A. (1998) Mol. Pharmacol. 54, 364-371). To characterize the functional group in CCK that interacts with His(207), we first substituted His(207) to Ala. This mutation decreased the affinity and the potency of CCK to produce total inositol phosphates 302-fold and 456… CONTINUE READING

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