1I5J
NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS
Summary for 1I5J
| Entry DOI | 10.2210/pdb1i5j/pdb |
| Descriptor | APOLIPOPROTEIN CII (1 entity in total) |
| Functional Keywords | protein-lipid interaction, amphipathic alpha helix, lipid transport |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 8921.86 |
| Authors | MacRaild, C.A.,Hatters, D.M.,Howlett, G.J.,Gooley, P.R. (deposition date: 2001-02-27, release date: 2001-05-16, Last modification date: 2024-05-22) |
| Primary citation | MacRaild, C.A.,Hatters, D.M.,Howlett, G.J.,Gooley, P.R. NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate. Biochemistry, 40:5414-5421, 2001 Cited by PubMed Abstract: The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous and largely disordered, with the rest of the protein forming a predominantly helical structure. Three regions of helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints, with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shed light on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation. PubMed: 11331005DOI: 10.1021/bi002821m PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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