In silico analysis of potential inhibitors of Ca2+ activated K+ channel blocker, Charybdotoxin-C from Leiurus quinquestriatus hebraeus through molecular docking and dynamics studies (Record no. 23759)

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003 - CONTROL NUMBER IDENTIFIER
control field OSt
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20251209122033.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 251209b |||||||| |||| 00| 0 eng d
040 ## - CATALOGING SOURCE
Original cataloging agency AIKTC-KRRC
Transcribing agency AIKTC-KRRC
100 ## - MAIN ENTRY--PERSONAL NAME
Author Kumar, R. Barani
9 (RLIN) 27720
245 ## - TITLE STATEMENT
Title In silico analysis of potential inhibitors of Ca2+ activated K+ channel blocker, Charybdotoxin-C from Leiurus quinquestriatus hebraeus through molecular docking and dynamics studies
250 ## - EDITION STATEMENT
Volume, Issue number Vol.47(3), May-Jun
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Place of publication, distribution, etc. Mumbai
Name of publisher, distributor, etc. Wolter Kluwer
Year 2015
300 ## - PHYSICAL DESCRIPTION
Pagination 280-284p.
520 ## - SUMMARY, ETC.
Summary, etc. Charybdotoxin-C (ChTx-C), from the scorpion Leiurus, quinquestriatus hebraeus blocks the calcium-activated potassium channels and causes hyper excitability of the nervous system. Detailed understanding the structure of ChTx-C, conformational stability, and intermolecular interactions are required to select the potential inhibitors of the toxin.<br/>Materials and Methods: <br/><br/>The structure of ChTx-C was modeled using Modeller 9v7. The amino acid residues lining the binding site were predicted and used for toxin-ligand docking studies, further, selected toxin-inhibitor complexes were studied using molecular dynamics (MD) simulations.<br/>Results: <br/><br/>The predicted structure has 91.7% of amino acids in the core and allowed regions of Ramachandran plot. A total of 133 analog compounds of existing drugs for scorpion bites were used for docking. As a result of docking, a list of compounds was shown good inhibiting properties with target protein. By analyzing the interactions, Ser 15, Lys 32 had significant interactions with selected ligand molecules and Val5, which may have hydrophobic interaction with the cyclic group of the ligand. MD simulation studies revealed that the conformation and intermolecular interactions of all selected toxin-inhibitor complexes were stable.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PHARMACOLOGY
9 (RLIN) 4774
700 ## - ADDED ENTRY--PERSONAL NAME
Co-Author Shanmuga, Priya B.
9 (RLIN) 27721
773 0# - HOST ITEM ENTRY
Place, publisher, and date of publication Andheri - Mumbai Wolters Kluwer India Private Limited
Title Indian Journal of Pharmacology
International Standard Serial Number 0253-7613
856 ## - ELECTRONIC LOCATION AND ACCESS
URL https://journals.lww.com/iphr/fulltext/2015/47030/in_silico_analysis_of_potential_inhibitors_of_ca2_.8.aspx
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