1EQ1
NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA APOLIPOPHORIN-III
Summary for 1EQ1
| Entry DOI | 10.2210/pdb1eq1/pdb |
| Related | 1AEP 1LPE |
| Descriptor | APOLIPOPHORIN-III (1 entity in total) |
| Functional Keywords | five helix-bundle, "helix-short helix-helix" recognition motif, lipid binding protein |
| Biological source | Manduca sexta (tobacco hornworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 18409.36 |
| Authors | Wang, J.,Sykes, B.D.,Ryan, R.O. (deposition date: 2000-03-31, release date: 2002-02-13, Last modification date: 2024-05-22) |
| Primary citation | Wang, J.,Sykes, B.D.,Ryan, R.O. Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein Proc.Natl.Acad.Sci.USA, 99:1188-1193, 2002 Cited by PubMed Abstract: The high-resolution NMR structure of apolipophorin III from the sphinx moth, Manduca sexta, has been determined in the lipid-free state. We show that lipid-free apolipophorin III adopts a unique helix-bundle topology that has several characteristic structural features. These include a marginally stable, up-and-down helix bundle that allows for concerted opening of the bundle about "hinged" loops upon lipid interaction and buried polar/ionizable residues and buried interhelical H-bonds located in the otherwise hydrophobic interior of the bundle that adjust protein stability and facilitate lipid-induced conformational opening. We suggest that these structural features modulate the conformational adaptability of the lipid-free helix bundle upon lipid binding and control return of the open conformation to the original lipid-free helix-bundle state. Taken together, these data provide a structural rationale for the ability of exchangeable apolipoproteins to reversibly interact with circulating lipoprotein particles. PubMed: 11818551DOI: 10.1073/pnas.032565999 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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