Magdalena Schacherl, Ulrich Baumann Structure

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Feeding Anthrax: The Crystal Structure of Bacillus anthracis InhA Protease Magdalena Schacherl, Ulrich Baumann Structure Volume 24, Issue 1, Pages 1-2 (January 2016) DOI: 10.1016/j.str.2015.12.002 Copyright © 2016 Elsevier Ltd Terms and Conditions

Figure 1 Biological Functions of B. anthracis InhA Protease (A) InhA influences many pathways in the human body by either cleaving proteins directly, like vWF, ADAMTS13, and ZO-1, or by influencing their induction. (B) InhA modulates about half of the secretome of B. anthracis, degrades extracellular matrix (ECM) proteins and plasma proteins, and cleaves B. anthracis S-layer protein BslA, consequently mediating motility of the pathogen. Structure 2016 24, 1-2DOI: (10.1016/j.str.2015.12.002) Copyright © 2016 Elsevier Ltd Terms and Conditions