NMR Studies of Human Apolipoprotein-E
EMSL Project ID
2128a
Abstract
This research proposal is centered on NMR structural studies of human apolipoprotein-E (apoE). ApoE plays important roles in several human diseases, including atherosclerosis and Alzheimer's diseases. Although the X-ray crystal structure of apoE N-terminal domain is available, there is no other structures reported to date. We solved the aggregation problem of apoE and prepared a full-length apoE that is monomeric and biologically active. We collected initial preliminary NMR data of this monomeric apoE, showing high-quality NMR spectra. In this proposal, we request NMR time on high-field NMR instrument to collect 3D/4D-NMR data for a complete assignment, since apoE is a 299-residue alpha-helical protein. We anticipate that a NMR structure of the intact apoE may provide answers to the structural basis of apoE's diverse functions.
Project Details
Project type
Capability Research
Start Date
2005-11-22
End Date
2006-04-03
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Chen B, X Ren, T Neville, WG Jerome, DW Hoyt, DL Sparks, G Ren, and J Wang. 2009. "Apolipoprotein AI tertiary structures determine stability and phospholipid-binding activity of discoidal high-density lipoprotein particles of different sizes." Protein Science 18(5):921-935. doi:10.1002/pro.101