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Fragment-based identification of determinants of conformational and spectroscopic change at the ricin active site |
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| Authors: | John H Carra Colleen A McHugh Sheila Mulligan LeeAnn M Machiesky Alexei S Soares Charles B Millard |
| Affiliation: | (1) United States Army Medical Research Institute of Infectious Diseases, 1425 Porter St., Fort Detrick, MD 21702, USA;(2) The Johns Hopkins Bloomberg School of Public Health, Department of Molecular Microbiology & Immunology, 615 N. Wolfe St., Baltimore, MD 21205, USA;(3) Mount St. Mary's University, 16300 Old Emmitsburg Rd., Emmitsburg, MD 21727, USA;(4) Goldbelt Raven LLC, 10 North Jefferson St., Suite 302, Frederick, MD 21701, USA;(5) Biology Department, 463, Brookhaven National Laboratory, Upton, NY 11973-5000, USA;(6) Walter Reed Army Institute of Research, Division of Biochemistry, 503 Robert Grant Ave., Silver Spring, MD 20910, USA |
| Abstract: | BackgroundRicin is a potent toxin and known bioterrorism threat with no available antidote. The ricin A-chain (RTA) acts enzymatically to cleave a specific adenine base from ribosomal RNA, thereby blocking translation. To understand better the relationship between ligand binding and RTA active site conformational change, we used a fragment-based approach to find a minimal set of bonding interactions able to induce rearrangements in critical side-chain positions. |
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