2LIX

Solution structure Analysis of the ImKTx104

Summary for 2LIX

• Entry DOI: 10.2210/pdb2lix/pdb
• NMR Information: BMRB: 17908
• Descriptor: Potassium Channel Toxins (1 entity in total)
• Functional Keywords: disulfide bond stabilized structure, toxin
• Biological source: Lychas mucronatus (Chinese swimming scorpion)
• Total number of polymer chains: 1
• Total formula weight: 2929.46

Authors

Zeng, D.Y.,Jiang, L. (deposition date: 2011-09-01, release date: 2012-07-25, Last modification date: 2024-10-30)

Primary citation

Chen, Z.Y.,Zeng, D.Y.,Hu, Y.T.,He, Y.W.,Pan, N.,Ding, J.P.,Cao, Z.J.,Liu, M.L.,Li, W.X.,Yi, H.,Jiang, L.,Wu, Y.L.
Structural and functional diversity of acidic scorpion potassium channel toxins.
Plos One, 7:e35154-e35154, 2012

PubMed Abstract: Although the basic scorpion K(+) channel toxins (KTxs) are well-known pharmacological tools and potential drug candidates, characterization the acidic KTxs still has the great significance for their potential selectivity towards different K(+) channel subtypes. Unfortunately, research on the acidic KTxs has been ignored for several years and progressed slowly.

PubMed: 22511981
DOI: 10.1371/journal.pone.0035154

Experimental method

SOLUTION NMR