期刊
CLINICAL LIPIDOLOGY
卷 4, 期 1, 页码 113-124出版社
FUTURE MEDICINE LTD
DOI: 10.2217/17584299.4.1.113
关键词
ApoA-I; cholesterol; cholesteryl ester; HDL; lecithin:cholesterol acyltransferase; phospholipid; protein structure; reverse cholesterol transport
资金
- NHLBI NIH HHS [R01 HL064163, R01 HL064163-08, P01 HL049373-160009, P01 HL049373] Funding Source: Medline
Lecithin:cholesterol acyltransferase (LCAT) is an enzyme that first hydrolyzes the sn-2 position of phospholipids, preferentially a diacylphosphocholine, and then transfers the fatty acid to cholesterol to yield a cholesteryl ester. HDL ApoA-I is the principal catalytic activator for LCAT. Activity of LCAT on nascent or lipid-poor HDL particles composed of phospholipid, cholesterol and ApoA-I allows the maturation of HDL particles into lipid-rich spherical particles that contain a core of cholesteryl ester surrounded by phospholipid and ApoA-I on the surface. This article reviews the recent progress in elucidating structural aspects of the interaction between LCAT and ApoA-I. In the last decade, there has been considerable progress in understanding the structure of ApoA-I and the central helices 5, 6, and 7 that are known to activate LCAT. However, much less information has been forthcoming describing the 3D structure and conformation of LCAT required to catalyze two separate reactions within a single monomeric peptide.
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