R
Roderick MacKinnon
Researcher at Howard Hughes Medical Institute
Publications - 190
Citations - 50997
Roderick MacKinnon is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Gating & Ion channel. The author has an hindex of 93, co-authored 180 publications receiving 47740 citations. Previous affiliations of Roderick MacKinnon include Beth Israel Deaconess Medical Center & Harvard University.
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Journal ArticleDOI
The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity
Declan A. Doyle,João H.Morais Cabral,Richard A. Pfuetzner,Anling Kuo,Jacqueline M. Gulbis,Steven L. Cohen,Brian T. Chait,Roderick MacKinnon +7 more
TL;DR: The architecture of the pore establishes the physical principles underlying selective K+ conduction, which promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter.
Journal ArticleDOI
Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K + Channel
TL;DR: In this paper, the authors reported the crystal structure of a mammalian voltage-dependent potassium ion (K+) channel, Kv1.2, which is a member of the Shaker K+ channel family.
Journal ArticleDOI
Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution.
TL;DR: Here it is shown how the K+ channel displaces water molecules around an ion at its extracellular entryway, and how it holds a K+ ion in a square antiprism of water molecules in a cavity near its intracellular entry way.
Journal ArticleDOI
X-ray structure of a voltage-dependent K+ channel
Youxing Jiang,Alice Lee,Jiayun Chen,Vanessa Ruta,Martine Cadene,Brian T. Chait,Roderick MacKinnon +6 more
TL;DR: The structure of KvAP, a voltage-dependent K+ channel from Aeropyrum pernix, is presented and a crystal structure of the full-length channel at a resolution of 3.2 Å is determined, which suggests that the voltage-sensor paddles move in response to membrane voltage changes, carrying their positive charge across the membrane.
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X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity.
TL;DR: This work presents the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 Å, respectively, and establishes the physical and chemical basis of their anion selectivity.