self-inhibited structure of full-length PCSK9 at 1.9 Å reveals structural homology with resistin within the C-terminal domain

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 104; no. 37; pp. 14604 - 14609
• Main Authors: Hampton, Eric N, Knuth, Mark W, Li, Jun, Harris, Jennifer L, Lesley, Scott A, Spraggon, Glen
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 11.09.2007; National Acad Sciences
• Subjects: Active sites; Amino Acid Sequence; Amino acids; Baculoviridae - genetics; Binding Sites; Biological Sciences; Blood; Blood plasma; Cardiovascular disease; Catalytic Domain; Cells; Crystal structure; Crystallography, X-Ray; Cysteine - chemistry; Cytokines; Disulfides; Disulfides - chemistry; Furin - chemistry; Genetic mutation; Histidine - chemistry; Hypercholesterolemia; Models, Chemical; Models, Molecular; Molecular Sequence Data; Molecules; Mutation; Oligopeptides - chemistry; Proprotein Convertase 9; Proprotein Convertases - chemistry; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Proteins; Receptors; Resistin - chemistry; Saccharomyces cerevisiae Proteins - chemistry; Sequence Homology, Amino Acid; Serine Endopeptidases - analysis; Serine Endopeptidases - chemistry; Serine Endopeptidases - genetics; Static Electricity

Mutations in proprotein convertase subtilisin/kexin type 9 (PCSK9) are strongly associated with levels of low-density lipoprotein cholesterol in the blood plasma and, thereby, occurrence or resistance to atherosclerosis and coronary heart disease. Despite this importance, relatively little is known...