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crystal structure of a charge engineered human lysozyme having enhanced bactericidal activity晶体结构的工程人工溶菌酶有增强杀菌活动
Crystal Structure of a Charge Engineered Human Lysozyme Having Enhanced Bactericidal Activity 1¤ 1 2 3,4 1,4,5 Avinash Gill , Thomas C. Scanlon , Daniel C. Osipovitch , Dean R. Madden , Karl E. Griswold * 1Thayer School of Engineering, Dartmouth College, Hanover, New Hampshire, United States of America, 2 Program in Experimental and Molecular Medicine, Dartmouth College, Hanover, New Hampshire, United States of America, 3 Department of Biochemistry, Dartmouth Medical School, Dartmouth College, Hanover, New Hampshire, United States of America, 4 Program in Molecular and Cellular Biology, Dartmouth College, Hanover, New Hampshire, United States of America, 5 Department of Biological Sciences, Dartmouth College, Hanover, New Hampshire, United States of America Abstract Human lysozyme is a key component of the innate immune system, and recombinant forms of the enzyme represent promising leads in the search for therapeutic agents able to treat drug-resistant infections. The wild type protein, however, fails to participate effectively in clearance of certain infections due to inherent functional limitations. For example, wild type lysozymes are subject to electrostatic sequestration and inactivation by anionic biopolymers in the infected airway. A charge engineered variant of human lysozyme has recently been shown to possess improved antibacterial activity in the ˚ presence of disease associated inhibitory molecules. Here, the 2.04 A crystal structure of this variant is presented along with an analysis that provides molecular level insights into the origins of the pro
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