Insights into the anthrax lethal factor–substrate interaction and selectivity using docking and molecular dynamics simulations

The anthrax toxin of the bacterium Bacillus anthracis consists of three distinct proteins, one of which is the anthrax lethal factor (LF). LF is a gluzincin Zn‐dependent, highly specific metalloprotease with a molecular mass of ∼90 kDa that cleaves most isoforms of the family of mitogen‐activated pr...

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Veröffentlicht in:	Protein science 2009-08, Vol.18 (8), p.1774-1785
Hauptverfasser:	Dalkas, Georgios A., Papakyriakou, Athanasios, Vlamis‐Gardikas, Alexios, Spyroulias, Georgios A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence anthrax lethal factor Antigens, Bacterial - chemistry Antigens, Bacterial - metabolism Bacillus anthracis - chemistry Bacillus anthracis - enzymology Bacterial Toxins - chemistry Bacterial Toxins - metabolism Binding Sites - physiology Catalytic Domain - physiology Computer Simulation Crystallography, X-Ray Databases, Protein docking enzyme‐substrate interactions MEK Mitogen-Activated Protein Kinase Kinases - chemistry Mitogen-Activated Protein Kinase Kinases - metabolism MKK molecular dynamics Molecular Sequence Data protein plasticity Protein Structure, Tertiary Structure-Activity Relationship Substrate Specificity Zinc - metabolism
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