Crystal structure of a charge engineered human lysozyme having enhanced bactericidal activity

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 infectio...

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Veröffentlicht in:	PloS one 2011-03, Vol.6 (3), p.e16788
Hauptverfasser:	Gill, Avinash, Scanlon, Thomas C, Osipovitch, Daniel C, Madden, Dean R, Griswold, Karl E
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - metabolism Amino acids Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Antibacterial activity Antibacterial agents Automation Bacteria Bacterial infections Bactericidal activity Biocatalysis - drug effects Biochemistry Biology Biopolymers Catalysis Cellular biology Chemical compounds Chronic obstructive pulmonary disease Collaboration Computational chemistry Crystal structure Crystallography Crystallography, X-Ray Cystic fibrosis Deactivation Deoxyribonucleic acid DNA Drug resistance Electrostatic properties Engineering Engineering schools Enzyme Stability - drug effects Enzymes Health aspects Humans Immune clearance Immune system Inactivation Infection Infections Innate immunity Ligands Lysozyme Microbial drug resistance Models, Molecular Mortality Muramidase - antagonists & inhibitors Muramidase - chemistry Muramidase - metabolism Muramidase - pharmacology Mutant Proteins - chemistry Mutation Pharmacology Pneumonia Protein Engineering Protein Processing, Post-Translational - drug effects Proteins Residues Respiratory tract Sequence Analysis, Protein Solvents Static Electricity Structural stability Surface active agents
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