3LNM
F233W mutant of the Kv2.1 paddle-Kv1.2 chimera channel
Summary for 3LNM
Entry DOI | 10.2210/pdb3lnm/pdb |
Related | 2R9R |
Descriptor | Voltage-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 Keywords | voltage-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 source | Rattus norvegicus (brown rat,rat,rats) More |
Cellular location | Cytoplasm : P62483 Cell membrane ; Multi-pass membrane protein : P63142 |
Total number of polymer chains | 4 |
Total formula weight | 204042.48 |
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 citation | Tao, 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: 20360102DOI: 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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