期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 25, 页码 11352-11357出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1000142107
关键词
anisotropic B factors; ion channel; normal-mode refinement; voltage gating
资金
- National Institutes of Health [R01-GM067801, R01-AI067839]
- National Science Foundation [MCB-0818353]
- Welch Foundation [Q-1512]
- American Heart Association [0865186F]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0818353] Funding Source: National Science Foundation
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 angstrom, has about 37% molecular mass of the transmembrane portion not resolved. In this study, by applying a novel normal-mode-based X-ray crystallographic refinement method to the original diffraction data and structural model, we established the structure of full-length Kv1.2 in its native form. This structure offers mechanistic insights into voltage sensing. Particularly, it shows a hydrophobic layer of about 10 angstrom at the midpoint of the membrane bilayer, which is likely the molecular basis for the observed focused electric field of Kv1.2 between the internal and external solutions. This work also demonstrated the potential of the refinement method in bringing up large chunks of missing densities, thus beneficial to structural refinement of many difficult systems.
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