Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca²⁺-dependent regulation of polycystin-2 channel activity

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 107; no. 20; pp. 9176 - 9181
• Main Authors: Petri, Edward T, Ćelić, Andjelka, Kennedy, Scott D, Ehrlich, Barbara E, Boggon, Titus J, Hodsdon, Michael E
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 18.05.2010; National Acad Sciences
• Subjects: Amino Acid Sequence; Autosomal dominant polycystic kidney; autosomal dominant polycystic kidney disease; Biological Sciences; Calcium; Calcium - metabolism; Chemical equilibrium; Conserved Sequence - genetics; Coordinate systems; EF hand motifs; EF Hand Motifs - genetics; Humans; hydrophobicity; Invertebrates; Models, Molecular; Molecular Sequence Data; nuclear magnetic resonance spectroscopy; Nuclear Magnetic Resonance, Biomolecular; Physiological regulation; Polycystic kidney diseases; Polycystic Kidney Diseases - genetics; Polycystic Kidney Diseases - metabolism; polycystins; Protein Conformation; Proteins; Sea urchins; Sequence Homology; TRPP Cation Channels - chemistry; TRPP Cation Channels - metabolism

The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca²⁺-permeable channel, is frequently mutated or truncated in autosomal dominant polycystic kidney disease. We have previously shown that this tail consists of three functional regions: an EF-hand domain (PC2-EF, 720-797), a flexible lin...