Importance of polarity of the α4-α5 loop residue - Asn 166 in the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: Implications for ion permeation and pore opening

Biochimica et Biophysica Acta - Biomembranes

Volumn 1838, Issue 1 PARTB, 2014, Pages 319-327

  Juntadech, Thanate ^a   Kanintronkul, Yodsoi ^a   Kanchanawarin, Chalermpol ^c   Katzenmeier, Gerd ^a   Angsuthanasombat, Chanan ^a,b  

^a MAHIDOL UNIVERSITY   (Thailand)

^b Laboratory of Molecular Biophysics and Structural Biochemistry   (Thailand)

^c KASETSART UNIVERSITY   (Thailand)

Author keywords

Bacillus thuringiensis; Cry endotoxins; Dye leakage assay; MD simulations; Planar lipid bilayers; Trimeric pore

Indexed keywords

ASPARAGINE; BACILLUS THURINGIENSIS TOXIN; CALCEIN; CRY4BA TOXIN; POTASSIUM CHANNEL; UNCLASSIFIED DRUG;

ALPHA HELIX; ALPHA4 ALPHA5 LOOP RESIDUE; ARTICLE; BACILLUS THURINGIENSIS; BACTERIUM MUTANT; CELL MEMBRANE; CHANNEL GATING; CONTROLLED STUDY; CRYSTAL STRUCTURE; FAST PROTEIN LIQUID CHROMATOGRAPHY; INSECTICIDAL ACTIVITY; ION TRANSPORT; LIPID BILAYER; LIPID VESICLE; MEMBRANE CONDUCTANCE; MEMBRANE TRANSPORT; MIDGUT; MOLECULAR DYNAMICS; NONHUMAN; PATCH CLAMP; PORE FORMING DOMAIN; PRIORITY JOURNAL; RESIDUE ANALYSIS; TOXIN STRUCTURE; WILD TYPE;

EID: 84887866677     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.10.002     Document Type: Article

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