Article
The self-inhibited structure of full-length PCSK9 at 1.9 A reveals structural homology with resistin within the C-terminal domain.
Proceedings of the National Academy of Sciences of the United States of America - 11 Sept 2007
Hampton Eric N, Knuth Mark W, Li Jun, Harris Jennifer L, Lesley Scott A, Spraggon Glen
Abstract excerpt
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 about the biology of PCSK9. Here, the crystal structure of a full-length construct of PCSK9 solved to 1.9-A...
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