2K4U

Solution structure of the SCORPION TOXIN ADWX-1

Summary for 2K4U

• Entry DOI: 10.2210/pdb2k4u/pdb
• Descriptor: Potassium channel toxin alpha-KTx 3.6 (1 entity in total)
• Functional Keywords: kv1.1 channel, kv1.3 channel, channel turret, adwx-1 peptide selectivity, structural basis, amidation, ionic channel inhibitor, neurotoxin, potassium channel inhibitor, secreted, toxin
• Biological source: Mesobuthus martensii (Chinese scorpion)
• Cellular location: Secreted: Q9NII7
• Total number of polymer chains: 1
• Total formula weight: 4088.98

Authors

Yin, S.J.,Jiang, L.,Yi, H.,Han, S.,Yang, D.W.,Liu, M.L.,Liu, H.,Cao, Z.J.,Wu, Y.L.,Li, W.X. (deposition date: 2008-06-18, release date: 2008-12-09, Last modification date: 2024-11-13)

Primary citation

Yin, S.J.,Jiang, L.,Yi, H.,Han, S.,Yang, D.W.,Liu, M.L.,Liu, H.,Cao, Z.J.,Wu, Y.L.,Li, W.X.
Different Residues in Channel Turret Determining the Selectivity of ADWX-1 Inhibitor Peptide between Kv1.1 and Kv1.3 Channels
J.Proteome Res., 7:4890-4897, 2008

PubMed Abstract: The low selectivity of Kv1 peptide inhibitors for specific isoforms makes them poor candidates for the development of theraputics. Using combined approaches, we showed that the Kv1 turret is the critical determinant for ADWX-1 peptide inhibitor selectivity of Kv1.3 over Kv1.1. Mutation of Kv1.1 turret residues to match the sequence of Kv1.3 lead to increased inhibition of Kv1.1 activity. These studies may lead to improvements in peptide inhibitor drug development.

PubMed: 18937510
DOI: 10.1021/pr800494a

Experimental method

SOLUTION NMR