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• W2096476280 startingPage "2255" @default.
• W2096476280 abstract "Having inspected the crystal structure of the complete KvAP channel protein, we suspect that the voltage-sensing domain is too distorted to provide reliable information about its native tertiary structure or its interactions with the central pore-forming domain. On the other hand, a second crystal structure of the isolated voltage-sensing domain may well correspond to a native open conformation. We also observe that the paddle model of gating developed from these two structures is inconsistent with many experimental results, and suspect it to be energetically unrealistic. Here we show that the isolated voltage-sensing domain crystal structure can be docked onto the pore domain portion of the full-length KvAP crystal structure in an energetically favorable way to create a model of the open conformation. Using this as a starting point, we have developed rather conventional models of resting and transition conformations based on the helical screw mechanism for the transition from the open to the resting conformation. Our models are consistent with both theoretical considerations and experimental results." @default.
• W2096476280 created "2016-06-24" @default.
• W2096476280 creator A5007171355 @default.
• W2096476280 creator A5010544263 @default.
• W2096476280 creator A5039866467 @default.
• W2096476280 date "2004-10-01" @default.
• W2096476280 modified "2023-09-23" @default.
• W2096476280 title "A Model of Voltage Gating Developed Using the KvAP Channel Crystal Structure" @default.
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• W2096476280 doi "https://doi.org/10.1529/biophysj.104.040592" @default.
• W2096476280 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1304651" @default.
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• W2096476280 hasPublicationYear "2004" @default.
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