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Descripción
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| Most voltage-gated potassium channels show strict rectification behavior: either they open upon membrane depolarization and mediate K+-efflux (e.g. Kv or plant Kout channels) or they open upon hyperpolarization and mediate K+-influx, only (e.g. HCN or plant Kin channels). Up to now it is not clear, however, how the different rectification properties are achieved. All these channels share a similar global tetrameric architecture with each of the four subunits having a voltage-sensing module, built of four transmembrane domains, and a pore module, formed by 2 transmembrane domains and a selectivity filter in between. In our study we took the plant Kin and Kout channel prototypes KAT1 and SKOR from Arabidopsis thaliana as starting point. KAT1 and SKOR share 29% identity at the amino acid level. On the basis of KAT1 we could generate the synthetic functional Kin channel SKIN.1 and on the basis of SKOR the synthetic functional Kout channel SKOUT.1. SKIN.1 and SKOUT.1 share 83% identity but still exhibit opposite rectification behavior. In further trial-and-error optimizations exploiting information from data bases on polymorphic protein sites, for instance, we could meanwhile generate SKIN.4 and SKOUT.4, which share 91% identity and which serve as inward rectifier and outward rectifier, respectively. The goal is to swap further sites in order to pinpoint those regions that are essential for the respective rectification property. | |
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Internacional
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Si |
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Nombre congreso
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Ion Channels in the Valley III |
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Tipo de participación
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960 |
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Lugar del congreso
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Montegrande at Valle del Elqui, Chile |
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Revisores
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Si |
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ISBN o ISSN
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0000-0000 |
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DOI
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Fecha inicio congreso
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08/04/2015 |
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Fecha fin congreso
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10/04/2015 |
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Desde la página
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0 |
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Hasta la página
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0 |
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Título de las actas
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The synthetic voltage-gated K+ channels SKIN and SKOUT share >90% identity but exhibit opposite rectification behavior |