Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States; Department of Cardiology, Howard Hughes Medical Institute, Boston Children’s Hospital, Boston, United States
Zongli Li
Department of Biological Chemistry and Molecular Pharmacology, Howard Hughes Medical Institute, Harvard Medical School, Boston, United States
Rick K Huang
Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States
Jin Zhang
Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States; School of Basic Medical Sciences, Nanchang University, Nanchang, China
Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States; Department of Cardiology, Howard Hughes Medical Institute, Boston Children’s Hospital, Boston, United States
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.
