Three-dimensional models of HDL apoA-I: implications for its assembly and function. J Lipid Res 2008 Sep;49(9):1875-83
Date
06/03/2008Pubmed ID
18515783Pubmed Central ID
PMC2515525DOI
10.1194/jlr.R800010-JLR200Scopus ID
2-s2.0-53149092105 (requires institutional sign-in at Scopus site) 95 CitationsAbstract
The purpose of this review is to highlight recent advances toward the refinement of a three-dimensional structure for lipid-bound apolipoprotein A-I (apoA-I) on recombinant HDL. Recently, X-ray crystallography has yielded a new structure for full-length, lipid-free apoA-I. Although this approach has not yet been successful in solving the three-dimensional structure of lipid-bound apoA-I, analysis of the X-ray structures has been of immense help in the interpretation of structural data obtained from other methods that yield structural information. Recent studies emphasize the use of mass spectrometry to unambiguously identify cross-linked peptides or to quantify solvent accessibility using hydrogen-deuterium exchange. The combination of mass spectrometry, molecular modeling, molecular dynamic analysis, and small-angle X-ray diffraction has provided additional structural information on apoA-I folding that complements previous approaches.
Author List
Thomas MJ, Bhat S, Sorci-Thomas MGAuthors
Mary Sorci Thomas PhD Professor in the Medicine department at Medical College of WisconsinMichael J. Thomas PhD Professor in the Pharmacology and Toxicology department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Apolipoprotein A-ICholesterol
Computer Simulation
Deuterium Exchange Measurement
Methionine
Models, Molecular
Models, Structural
Oxidation-Reduction
Protein Conformation
Recombinant Proteins
