3LUT

A Structural Model for the Full-length Shaker Potassium Channel Kv1.2

Summary for 3LUT

• Entry DOI: 10.2210/pdb3lut/pdb
• Related: 2R9R
• Descriptor: Voltage-gated potassium channel subunit beta-2, Potassium voltage-gated channel subfamily A member 2, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• Functional Keywords: voltage gating, potassium channel, kv1.2, gating charges, normal-mode analysis, ion transport, ionic channel, nadp, phosphoprotein, potassium, potassium transport, transport, voltage-gated channel, glycoprotein, lipoprotein, membrane, palmitate, transmembrane, membrane protein
• Biological source: Rattus norvegicus (Rat); More
• Cellular location: Cytoplasm (Potential): P62483; Membrane; Multi-pass membrane protein: P63142
• Total number of polymer chains: 2
• Total formula weight: 98812.68

Authors

Chen, X.,Ni, F.,Wang, Q.,Ma, J. (deposition date: 2010-02-18, release date: 2010-06-23, Last modification date: 2024-02-21)

Primary citation

Chen, X.,Wang, Q.,Ni, F.,Ma, J.
Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement.
Proc.Natl.Acad.Sci.USA, 107:11352-11357, 2010

PubMed Abstract: 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 A, 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 A 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.

PubMed: 20534430
DOI: 10.1073/pnas.1000142107

Experimental method

X-RAY DIFFRACTION (2.9 Å)