2OBD
Crystal Structure of Cholesteryl Ester Transfer Protein
Summary for 2OBD
| Entry DOI | 10.2210/pdb2obd/pdb |
| Descriptor | Cholesteryl ester transfer protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (9 entities in total) |
| Functional Keywords | cholesteryl ester, lipid transfer protein, lipid transport |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 57489.27 |
| Authors | |
| Primary citation | Qiu, X.,Mistry, A.,Ammirati, M.J.,Chrunyk, B.A.,Clark, R.W.,Cong, Y.,Culp, J.S.,Danley, D.E.,Freeman, T.B.,Geoghegan, K.F.,Griffor, M.C.,Hawrylik, S.J.,Hayward, C.M.,Hensley, P.,Hoth, L.R.,Karam, G.A.,Lira, M.E.,Lloyd, D.B.,McGrath, K.M.,Stutzman-Engwall, K.J.,Subashi, A.K.,Subashi, T.A.,Thompson, J.F.,Wang, I.K.,Zhao, H.,Seddon, A.P. Crystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid molecules. Nat.Struct.Mol.Biol., 14:106-113, 2007 Cited by PubMed Abstract: Cholesteryl ester transfer protein (CETP) shuttles various lipids between lipoproteins, resulting in the net transfer of cholesteryl esters from atheroprotective, high-density lipoproteins (HDL) to atherogenic, lower-density species. Inhibition of CETP raises HDL cholesterol and may potentially be used to treat cardiovascular disease. Here we describe the structure of CETP at 2.2-A resolution, revealing a 60-A-long tunnel filled with two hydrophobic cholesteryl esters and plugged by an amphiphilic phosphatidylcholine at each end. The two tunnel openings are large enough to allow lipid access, which is aided by a flexible helix and possibly also by a mobile flap. The curvature of the concave surface of CETP matches the radius of curvature of HDL particles, and potential conformational changes may occur to accommodate larger lipoprotein particles. Point mutations blocking the middle of the tunnel abolish lipid-transfer activities, suggesting that neutral lipids pass through this continuous tunnel. PubMed: 17237796DOI: 10.1038/nsmb1197 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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