Interhelical contacts are required for the helix bundle fold of apolipophorin III and its ability to interact with lipoproteins

Protein Science

Volumn 7, Issue 2, 1998, Pages 336-341

  Wang, Jianjun ^a   Narayanaswami, Vasanthy ^a   Sykes, Brian D ^a   Ryan, Robert O ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

Author keywords

Amphipathic apolipoprotein; Helix bundle; Nuclear magnetic resonance; helix

Indexed keywords

APOLIPOPHORIN III; APOLIPOPROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; DNA HELIX; LEPIDOPTERA; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

EID: 0031935716     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070213     Document Type: Article

References (30)

1. Bax A, Davis DG. 1985. MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy J Magn Reson 65:355-360.
2. Breiter DR, Kanost MR, Benning MM, Wesenberg G, Law JH, Wells MA, Rayment I, Holden HM. 1991. Molecular structure of an apolipoprotein determined at 2.5-Å resolution. Biochemistry 30:603-608.
3. Brünger AT. 1992. X-PLOR. A system for X-ray crystallography and NMR. New Haven, Connecticut: Yale University Press.
4. Hård K, Van Doom JM, Thomas-Oates JE, Kamerling JP, Van der Horst DJ. 1993. Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-amino-ethylphosphonate as a constituent of a glycoprotein. Biochemistry 32:766-775.
5. Henry GD, Sykes BD. 1994. Methods to study membrane protein structure in solution. Methods Enzymol 239:515-535.
6. Hickson-Bick D, Knapp RD, Sparrow JT, Sparrow DA, Gotto AM Jr. Massey JB, Pownall HJ. 1988. Kinetics and mechanism of transfer of synthetic model apolipoproteins. Biochemistry 27:7881-7886.
7. Jeener J, Meier BH, Bachmann P, Ernst RR. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy J Chem Phys 71:4546-4553.
8. Narayanaswami V, Kay CM, Oikawa K, Ryan RO. 1994. Structural and binding characteristics of the carboxyl terminal fragment of apolipophorin III from Manduca sexta. Biochemistry 33:13312-13320.
9. Narayanaswami V, Wang J, Kay CM, Scraba DG, Ryan RO. 1996. Disulfide bond engineering to monitor conformational opening ol apolipophorin III during lipid binding. J Biol Chem 271:26855-26862.
10. Narayanaswami V, Weers PMM, Bogerd J, Kooiman FP, Kay CM, Scraba DG, Van der Horst DJ, Ryan RO. 1995. Spectroscopic and lipid binding studies on the amino and carboxyl terminal fragments of Locusta migratoria apolipophorin III. Biochemistry 34:11822-11830.
11. Nigles M, Clore GM, Gronenborn AM. 1988. Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. FEBS Lett 229:129-136.
12. 1H NMR spectra of proteins via double quantum filtering. Biochem Biophys Res Commun 117:479-485.
13. Ryan RO. 1990. Dynamics of insect lipophorin metabolism. J Lipid Res 31:1725-1739.
14. Ryan RO. 1996. Structural studies of lipoproteins and their apolipoprotein components. Biochem Cell Biol 74:155-174.
15. Segrest JP, De Loof H, Dohlman JG, Brouillette CG, Anantharamaiah GM. 1990. Amphipathic helix motif: Classes and properties. Proteins Struct Funct Genet 8:103-117.
16. Segrest JP, Garber DW, Brouillette CG, Harvey SC, Anantharamaiah GM. 1994. The amphipathic alpha helix: A multifunctional structural motif in plasma apolipoproteins. Adv Protein Chem 45:303-369.
17. Segrest JP, Jones MK, De Loof H, Brouillette CG, Venkatachalapathi YV, Anantharamaiah GM. 1992. The amphipathic helix in the exchangeable apolipoproteins: A review of secondary structure and function. J Lipid Res 33:141-166.
18. Sönnichsen FD, Van Eyk JE, Hodges RS, Sykes BD. 1992. Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide. Biochemistry 31:8790-8798.
19. Soulages JL, Salamon Z, Wells MA, Tollin G. 1995. Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: A surface plasmon resonance spectroscopy study. Proc Natl Acad Sci USA 92:5650-5654.
20. Sparrow JT, Sparrow DA, Fernando G, Culwell AR, Kovar M, Gotto AM Jr. 1992. Apolipoprotein E: Phospholipid binding studies with synthetic peptides from the carboxyl terminus. Biochemistry 31:1065-1068.
21. Wang G, Pierens GK, Treleaven WD, Sparrow JT, Cushley RJ. 1996a. Conformations of hman apolipoprotein E(263-286) and E(267-289) in aqueous solutions of sodium dodecyl sulfate by CD and 1H-NMR. Biochemistry 35:10358-10366.
22. 1H-NMR and CD. Evidence for specific peptide SDS interactions. Biochim Biophys Acata 1301:174-184.
23. Wang J, Gagne SM, Sykes BD, Ryan RO. 1997. Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional heteronuclear NMR techniques. J Biol Chem 272:17912-17921.
24. Wang J, Hodges RS, Sykes BD. 1995. Effect of trifluoroethanol on the solution structure and flexibility of desmopressin: A two-dimensional NMR study. Int J Peptide Protein Res 45:471-481.
25. Wientzek M, Kay CM, Oikawa K, Ryan RO. 1994. Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change. J Biol Chem 269:4605-4612.
26. Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. 1991. Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science 252:1817-1822.
27. Wishart DS, Boyko R, Willard L, Richards FM, Sykes BD. 1994a. SEQSEE: A comprehensive program suite for protein sequence analysis. CABIOS 10:121-132.
28. Wishart DS, Sykes BD, Richards FM. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333.
29. Wishart DS, Willard L, Richards FM, Sykes BD. 1994b. VADAR: A comprehensive program for protein structure evaluation. Version 1.2. Edmonton, Alberta, Canada.
30. Wüthrich K. 1986. NMR of proteins and nucleic acids. New York: John Wiley & Sons. pp 162-166.