Cryo-EM structure of the polycystin 2-l1 ion channel

  • Elife. 2018 Jul 13;7:e36931. doi: 10.7554/eLife.36931.
Raymond E Hulse  1  2 ,  Zongli Li  3 ,  Rick K Huang  1 ,  Jin Zhang  1  4 ,  David E Clapham  1  2
Affiliations
  • 1. Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.
  • 2. Department of Cardiology, Howard Hughes Medical Institute, Boston Children's Hospital, Boston, United States.
  • 3. Department of Biological Chemistry and Molecular Pharmacology, Howard Hughes Medical Institute, Harvard Medical School, Boston, United States.
  • 4. School of Basic Medical Sciences, Nanchang University, Nanchang, China.
PMID: 30004384 DOI: 10.7554/eLife.36931
Abstract

We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel. Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes. The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics. Here we show that these differences are reflected in the architecture of polycystin 2-l1.

Keywords
PC-2L1; TRP channel; calcium; cryo-EM; human; molecular biophysics; primary cilia; structural biology.