Structure and Function of the Bestrophin family of calcium-activated chloride channels
| Autor: | Aaron P. Owji, Yu Zhang, Alec Kittredge, Tingting Yang |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Bestrophins
Biophysics Reviews Review Gating bestrophin structure Crystallography X-Ray Biochemistry Chloride Channels Calcium-Activated Chloride Channels Animals Humans Patch clamp Eye Proteins biology Chemistry Bestrophin function Electrophysiological Phenomena Cell biology Structure and function Bestrophin 1 Structural biology Chloride channel biology.protein Calcium Cattle Best2 Best1 |
| Zdroj: | Channels article-version (VoR) Version of Record |
| ISSN: | 1933-6969 1933-6950 |
| DOI: | 10.1080/19336950.2021.1981625 |
| Popis: | Bestrophins are a family of calcium-activated chloride channels (CaCCs) with relevance to human physiology and a myriad of eye diseases termed “bestrophinopathies”. Since the identification of bestrophins as CaCCs nearly two decades ago, extensive studies from electrophysiological and structural biology perspectives have sought to define their key channel features including calcium sensing, gating, inactivation, and anion selectivity. The initial X-ray crystallography studies on the prokaryotic homolog of Best1, Klebsiella pneumoniae (KpBest), and the Best1 homolog from Gallus gallus (chicken Best1, cBest1), laid the foundational groundwork for establishing the architecture of Best1. Recent progress utilizing single-particle cryogenic electron microscopy has further elucidated the molecular mechanism of gating in cBest1 and, separately, the structure of Best2 from Bos taurus (bovine Best2, bBest2). Meanwhile, whole-cell patch clamp, planar lipid bilayer, and other electrophysiologic analyses using these models as well as the human Best1 (hBest1) have provided ample evidence describing the functional properties of the bestrophin channels. This review seeks to consolidate these structural and functional results to paint a broad picture of the underlying mechanisms comprising the bestrophin family’s structure-function relationship. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|