Structurally conserved aromaticity of Tyr249 and Phe 264 in helix 7 is important for toxicity of the Bacillus thuringiensis Cry4Ba toxin

Functional elements of the conserved helix 7 in the poreforming domain of the Bacillus thuringiensis Cry δ-endotoxins have not yet been clearly identified. Here, we initially performed alanine substitutions of four highly conserved aromatic residues, Trp243, Phe246, Tyr 249 and Phe264, in helix 7 of...

Full description

Saved in:
Bibliographic Details
Main Authors: Kasorn Tiewsiri, Chanan Angsuthanasombat
Other Authors: Mahidol University
Format: Article
Published: 2018
Subjects:
Online Access:https://repository.li.mahidol.ac.th/handle/123456789/24234
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Mahidol University
Be the first to leave a comment!
You must be logged in first