Domain Structure and Lipid Interaction in Human Apolipoproteins A-I and E, a General Model
Dec 16, 2003
Chen-Ya Huang
Institute of Bioinformatics
Exchangeable apolipoproteins (apo) play important role in lipid transport and metabolism. This class of proteins, including human apoA and –E, have the same genomic structure and are of the same gene family. In this paper, a series of apoA-I variants were used to probe the structural organization and the different domains in lipid binding. From these observations, the authors conclude a two-step mechanism for lipid binding of apoA-I. Because of the structural similarity between apoA-I and other exchangeable apolipoproteins, such as apoE and apoA-IV, the two-step binding mechanism could be a general model for lipid interaction of other apolipoproteins comprising two domains.
Saito, H., Dhanasekaran, P., Nguyen, D., Holvoet, P., Lund-Katz, S. and Phillips, M. C. (2003) J. Biol. Chem. 278, 23227-23232.
http://www.jbc.org/cgi/content/abstract/278/26/23227
1. Li, W. H., Tanimura, M., Luo, C. C., Datta, S., and Chan, L. (1988) The apolipoprotein multigene family: Biosynthesis, Structure, Structure-function relationships, and evolution. J Lipid Res. 29, 245-271. Review.
2. Frank PG, Marcel YL.(2000) Apolipoprotein A-I: structure-function relationships. J Lipid Res. 41, 853-72. Review.
3. Saito, H., Dhanasekaran, P., Baldwin, F., Weisgraber, K. H., Lund-Katz, S., and Phillips, M. C. (2001) Lipid Binding-induced conformational Change in Human Apolipoprotein E. J. Biol. Chem. 276, 40949-40954.