Functional organization of the sortilin Vps10p domain.

@article{Westergaard2004FunctionalOO,
  title={Functional organization of the sortilin Vps10p domain.},
  author={Uffe B Westergaard and Esben Skipper S\orensen and Guido Hermey and Morten S Nielsen and Anders Nykjaer and Kirstine Kirkegaard and Christian Jacobsen and J\orgen Gliemann and Peder Madsen and Claus Munck Petersen},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 48},
  pages={50221-9}
}
A Vps10p domain makes up the entire luminal part of Sortilin, and this type of domain is the hallmark of a new family of neuronal receptors that target a variety of ligands, including neurotrophins and neuropeptides. We have shown that two structural features of the Vps10p domain, the N-terminal propeptide and the C-terminal segment of ten conserved cysteines (10CC), are key elements in the function of Sortilin. The propeptide has two functions. (i) It binds the mature part of Sortilin and… CONTINUE READING

From This Paper

Topics from this paper.

Similar Papers

Loading similar papers…