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Molecular Bases of Disease
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- Protein Structure and FoldingOpen Access
A Systematic Investigation of Structure/Function Requirements for the Apolipoprotein A-I/Lecithin Cholesterol Acyltransferase Interaction Loop of High-density Lipoprotein
Journal of Biological ChemistryVol. 291Issue 12p6386–6395Published online: January 21, 2016- Xiaodong Gu
- Zhiping Wu
- Ying Huang
- Matthew A. Wagner
- Camelia Baleanu-Gogonea
- Ryan A. Mehl
- and others
Cited in Scopus: 14The interaction of lecithin-cholesterol acyltransferase (LCAT) with apolipoprotein A-I (apoA-I) plays a critical role in high-density lipoprotein (HDL) maturation. We previously identified a highly solvent-exposed apoA-I loop domain (Leu159–Leu170) in nascent HDL, the so-called “solar flare” (SF) region, and proposed that it serves as an LCAT docking site (Wu, Z., Wagner, M. A., Zheng, L., Parks, J. S., Shy, J. M., 3rd, Smith, J. D., Gogonea, V., and Hazen, S. L. (2007) Nat. Struct. Mol. Biol. 14, 861–868).