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- W4254825248 abstract "Mutations of gating sensitive amino acids in pore-forming S6 segments may transform a high-voltage-activated into a low-voltage-activated calcium channel. Resulting disturbances in calcium entry can cause channelopathies. Here we analyze the role of physico-chemical properties of residues in the ‘bundle-crossing-region’ of helices IS6, IIS6 and IIIS6 in activation gating of Cav1.2. Gating sensitive L434, I781 and G1193 were substituted by residues of different size, hydrophobicity and polarity. Descriptors characterizing the various amino acid properties were calculated using the software package MOE or taken from literature. Most mutations induced leftward shifts of the activation curves and decelerated current activation and deactivation suggesting a destabilization of the closed and a stabilization of the open channel state. A selection of 17 physico-chemical parameters (descriptors) was calculated for these residues and examined for correlation with the shifts of the midpoints of the activation curve (Vact). Vact correlated with local side chain flexibility in position L434 (IS6), with the polar accessible surface area of the side chain in position G1193 (IIIS6) and with hydrophobicity in position I781 (IIS6). Combined descriptor analysis for positions I781 and G1193 revealed that additional amino acid properties may contribute to conformational changes during the gating process. The identified physicochemical properties in the analyzed gating sensitive positions predict the shifts of the activation curves of CaV1.2. Correlation analysis emerges as a useful tool to identify the impact of the different properties of amino acids on channel gating." @default.
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- W4254825248 date "2011-02-01" @default.
- W4254825248 modified "2023-10-18" @default.
- W4254825248 title "Physicochemical Properties of Pore Residues Predict Activation Gating of Cav1.2: A Correlation Mutation Analysis" @default.
- W4254825248 doi "https://doi.org/10.1016/j.bpj.2010.12.3297" @default.
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