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- W591328338 abstract "The structural basis of ion channel function remained mostly a mystery for more than 140 years since the existence of water-filled pores through membranes was first postulated (Brücke, 1843). Despite intense efforts in the determination of the electrophysiological properties of ion channels (for a review see Hille, 1992), starting with the seminal work of Hodgkin and Huxley, the field still suffers from the lack of high-resolution structures of ion channel proteins. The first determination of the structure of a membrane protein, the photosynthetic reaction center (Deisenhofer et al., 1985), was a flash of hope for the crystallization of membrane-integrated ion channel proteins in order to understand their selectivity, conductance regulation, and voltage-gating. But still, no crystals of ion channel proteins diffracting x-rays to high resolution could be obtained. Therefore, channel model systems with known crystal structures, such as the porins (e.g., Weiss et al., 1991) or colicins (e.g., Parker et al., 1989), were valuable. Unfortunately, these proteins do not combine the main features of typical ion channels mentioned above. To compensate for this shortcoming extensive investigations by mutational analysis (see Catterall, 1988 or Miller, 1991 for reviews) and molecular modeling (see Guy and Seetharamulu, 1992; Durell and Guy, 1992) of ion channels and of pore-forming peptides (see Sansom, 1991 for a review) were carried out. In 1990, annexin V was structurally characterized as the first ion channel protein, thus paving the way, in combination with electrophysiological analysis of annexin V mutants, for an understanding of ion channel function in molecular terms." @default.
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- W591328338 date "1995-01-01" @default.
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- W591328338 title "Annexin V: Structure-function analysis of a voltage-gated, calcium-selective ion channel" @default.
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- W591328338 doi "https://doi.org/10.1007/978-3-0348-9057-1_22" @default.
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