Solution structure of a K+-channel blocker from the scorpion Tityus cambridgei
β Scribed by Iren Wang; Shih-Hsiung Wu; Hsueh-Kai Chang; Ru-Chi Shieh; Hui-Ming Yu; Chinpan Chen
- Book ID
- 111753344
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2009
- Tongue
- English
- Weight
- 557 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0961-8368
- DOI
- 10.1110/ps.33402
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BmKTX is a toxin recently purified from the venom of Buthus Martensi, which belongs to the kaliotoxin family. We have determined its solution structure by use of conventional twodimensional NMR techniques followed by distancegeometry and energy minimization. The calculated structure is composed of a
TsKapa (TsK), purified from the Buthidae Tityus serrulatus is a very high potent ligand for small-conductance apaminsensitive calcium-activated potassium channels (SK). It is able to efficiently compete with apamin for binding on this channel (K 0.5 β«Ψβ¬ 0.3 nM) [Legros, C. et al., FEBS Lett. 390:81-