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3LNM

F233W mutant of the Kv2.1 paddle-Kv1.2 chimera channel

Summary for 3LNM
Entry DOI10.2210/pdb3lnm/pdb
Related2R9R
DescriptorVoltage-gated potassium channel subunit beta-2, F233W mutant of the Kv2.1 paddle-Kv1.2 chimera, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
Functional Keywordsvoltage-gated potassium channel-beta subunit complex, acetylation, cytoplasm, ion transport, ionic channel, nadp, phosphoprotein, potassium, potassium transport, transport, voltage-gated channel, glycoprotein, lipoprotein, membrane, palmitate, potassium channel, transmembrane, membrane protein, transport protein
Biological sourceRattus norvegicus (brown rat,rat,rats)
More
Cellular locationCytoplasm : P62483
Cell membrane ; Multi-pass membrane protein : P63142
Total number of polymer chains4
Total formula weight204042.48
Authors
Tao, X.,Lee, A.,Limapichat, W.,Dougherty, D.A.,MacKinnon, R. (deposition date: 2010-02-02, release date: 2010-04-14, Last modification date: 2023-09-06)
Primary citationTao, X.,Lee, A.,Limapichat, W.,Dougherty, D.A.,MacKinnon, R.
A gating charge transfer center in voltage sensors.
Science, 328:67-73, 2010
Cited by
PubMed Abstract: Voltage sensors regulate the conformations of voltage-dependent ion channels and enzymes. Their nearly switchlike response as a function of membrane voltage comes from the movement of positively charged amino acids, arginine or lysine, across the membrane field. We used mutations with natural and unnatural amino acids, electrophysiological recordings, and x-ray crystallography to identify a charge transfer center in voltage sensors that facilitates this movement. This center consists of a rigid cyclic "cap" and two negatively charged amino acids to interact with a positive charge. Specific mutations induce a preference for lysine relative to arginine. By placing lysine at specific locations, the voltage sensor can be stabilized in different conformations, which enables a dissection of voltage sensor movements and their relation to ion channel opening.
PubMed: 20360102
DOI: 10.1126/science.1185954
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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数据于2025-07-23公开中

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