Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 107; no. 25; pp. 11352 - 11357
• Main Authors: Chen, Xiaorui, Wang, Qinghua, Ni, Fengyun, Ma, Jianpeng, Lipscomb, William N.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 22.06.2010; National Acad Sciences
• Subjects: Animals; Anisotropy; Atoms; Binding Sites; Biological Sciences; Biophysics; Biosensors; Cell Membrane - metabolism; Chimeras; Crystal structure; Crystallography; Crystallography, X-Ray - methods; electric field; Electric fields; Electric potential; Electron density; Glycosylation; Hydrophobic and Hydrophilic Interactions; hydrophobicity; Ion channels; Ion Channels - chemistry; Kv1.2 Potassium Channel - chemistry; Lipid Bilayers - chemistry; Mammals; Membranes; Models, Molecular; Molecular Conformation; molecular weight; Molecules; Neurons; Potassium; Potassium channels; Protein Conformation; Protein Structure, Tertiary; Rats; Recombinant Fusion Proteins - chemistry; Sensors; X-ray diffraction; X-rays

Voltage-dependent potassium channels (Kv) are homotetramers composed of four voltage sensors and one pore domain. Because of high-level structural flexibility, the first mammalian Kv structure, Kv1.2 at 2.9 Å, has about 37% molecular mass of the transmembrane portion not resolved. In this study, by...