Chimeric structural stabilities in the coiled-coil structure of the NECK domain in human lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1)

Journal of Biochemistry

Volumn 141, Issue 6, 2007, Pages 855-866

  Ishigaki, Tomoko ^a   Ohki, Izuru ^a   Utsunomiya Tate, Naoko ^b   Tate, Shin Icih ^a,c,d  

^a BIOMOL ENG RESEARCH INSTITUTE   (Japan)

^b MUSASHINO UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Atherosclerosis; CD; LDL; Membrane proteins; NMR

Indexed keywords

MYOSIN; OXIDIZED LOW DENSITY LIPOPROTEIN RECEPTOR 1; HYBRID PROTEIN; LIGAND; LOW DENSITY LIPOPROTEIN; OXYGEN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL SURFACE; CHIMERA; CIRCULAR DICHROISM; CONTROLLED STUDY; LIGAND BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; OLIGOMERIZATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN STRUCTURE; AMINO ACID SEQUENCE; AORTA; ATHEROSCLEROSIS; CHEMISTRY; CONFORMATION; ENDOTHELIUM CELL; HUMAN; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AORTA; ATHEROSCLEROSIS; CIRCULAR DICHROISM; ENDOTHELIAL CELLS; HUMANS; LIGANDS; LIPOPROTEINS, LDL; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; OXYGEN; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SCAVENGER RECEPTORS, CLASS E; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 38449100736     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm093     Document Type: Article

References (43)

1. Chen, M., Masaki, T., and Sawamura, T. (2002) LOX-1, the receptor for oxidized low-density lipoprotein identified from endothelial cells: implications in endothelial dysfunction and atherosclerosis. Pharmacol. Ther. 95, 89-100
2. Sawamura, T., Kume, N., Aoyama, T., Moriwaki, H., Hoshikawa, H., Aiba, Y., Tanaka, T., Miwa, S., Katsura, Y., Kita, T., and Masaki, T. (1997) An endothelial receptor for oxidized low-density lipoprotein. Nature 386, 73-77
3. Kita, T. (1999) LOX-1, a possible clue to the missing link between hypertension and atherogenesis. Circ. Res. 84, 1113-1115
4. Kita, T., Kume, N., Minami, M., Hayashida, K., Murayama, T., Sano, H., Moriwaki, H., Kataoka, H., Nishi, E., Horiuchi, H., Arai, H., and Yokode, M. (2001) Role of oxidized LDL in atherosclerosis. Ann. N.Y. Acad. Sci. 947, 199-206
5. Mehta, J.L. (2004) The role of LOX-1, a novel lectin-like receptor for oxidized low density lipoprotein, in atherosclerosis. Can. J. Cardiol. 20 (Suppl. B), 32B-36B
6. Kume, N., Murase, T., Moriwaki, H., Aoyama, T., Sawamura, T., Masaki, T., and Kita, T. (1998) Inducible expression of lectin-like oxidized LDL receptor-1 in vascular endothelial cells. Circ. Res. 83, 322-327
7. Mehta, J.L., Li, D.Y., Chen, H.J., Joseph, J., and Romeo, F. (2001) Inhibition of LOX-1 by statins may relate to upregulation of eNOS. Biochem. Biophys. Res. Commun. 289, 857-861
8. Mehta, J.L., Hu, B., Chen, J., and Li, D. (2003) Pioglitazone inhibits LOX-1 expression in human coronary artery endothelial cells by reducing intracellular superoxide radical generation. Arterioscler. Thromb. Vasc. Biol. 23, 2203-2208
9. Moriwaki, H., Kume, N., Kataoka, H., Murase, T., Nishi, E., Sawamura, T., Masaki, T., and Kita, T. (1998) Expression of lectin-like oxidized low density lipoprotein receptor-1 in human and murine macrophages: upregulated expression by TNF-alpha. FEBS Lett. 440, 29-32
10. Kakutani, M., Ueda, M., Naruko, T., Masaki, T., and Sawamura, T. (2001) Accumulation of LOX-1 ligand in plasma and atherosclerotic lesions of Watanabe heritable hyperlipidemic rabbits: identification by a novel enzyme immunoassay. Biochem. Biophys. Res. Commun. 282, 180-185
11. Kataoka, H., Kume, N., Miyamoto, S., Minami, M., Moriwaki, H., Murase, T., Sawamura, T., Masaki, T., Hashimoto, N., and Kita, T. (1999) Expression of lectinlike oxidized low-density lipoprotein receptor-1 in human atherosclerotic lesions. Circulation 99, 3110-3117
12. Xie, Q., Matsunaga, S., Niimi, S., Ogawa, S., Tokuyasu, K., Sakakibara, Y., and Machida, S. (2004) Human lectin-like oxidized low-density lipoprotein receptor-1 functions as a dimer in living cells. DNA Cell Biol. 23, 111-117
13. Ohki, I., Ishigaki, T., Oyama, T., Matsunaga, S., Xie, Q., Ohnishi-Kameyama, M., Murata, T., Tsuchiya, D., Machida, S., Morikawa, K., and Tate, S. (2005) Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL. Structure. (Camb.) 13, 905-917
14. Park, H., Adsit, F.G., and Boyington, J.C. (2005) The 1.4 angstrom crystal structure of the human oxidized low density lipoprotein receptor lox-1. J. Biol. Chem. 280, 13593-13599
15. Drickamer, K. and Dodd, R.B. (1999) C-Type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence. Glycobiology 9, 1357-1369
16. Yokoyama, W.M. and Plougastel, B.F. (2003) Immune functions encoded by the natural killer gene complex. Nat. Rev. Immunol. 3, 304-316
17. Drickamer, K. (1999) C-type lectin-like domains. Curr. Opin. Struct. Biol. 9, 585-590
18. Burkhard, P., Stetefeld, J., and Strelkov, S.V. (2001) Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 11, 82-88
19. Cohen, C. and Parry, D.A. (1990) Alpha-helical coiled coils and bundles: how to design an alpha-helical protein. Proteins 7, 1-15
20. Lupas, A. (1996) Coiled coils: new structures and new functions. Trends Biochem. Sci. 21, 375-382
21. Bernhard, O.K., Lai, J., Wilkinson, J., Sheil, M.M., and Cunningham, A.L. (2004) Proteomic analysis of DC-SIGN on dendritic cells detects tetramers required for ligand binding but no association with CD4. J. Biol. Chem. 279, 51828-51835
22. Weis, W.I. and Drickamer, K. (1994) Trimeric structure of a C-type mannose-binding protein. Structure. 2, 1227-1240
23. Chakrabartty, A., Schellman, J.A., and Baldwin, R.L. (1991) Large differences in the helix propensities of alanine and glycine. Nature 351, 586-588
24. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
25. Garrett, D.S., Powers, R., Gronenborn, A.M., and Clore, G.M. (1991) A common sense approach to peak picking in two-, three-, and fourdimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95, 214-220
26. Markley, J.L., Bax, A., Arata, Y., Hilbers, C.W., Kaptein, R., Sykes, B.D., Wright, P.E., and Wüthrich, K. (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. J. Biomol. NMR 12, 1-23
27. Nagase, M., Hirose, S., and Fujita, T. (1998) Unique repetitive sequence and unexpected regulation of expression of rat endothelial receptor for oxidized low-density lipoprotein (LOX-1). Biochem. J. 330 (Pt 3), 1417-1422
28. Kume, N. and Kita, T. (2001) Roles of lectin-like oxidized LDL receptor-1 and its soluble forms in atherogenesis. Curr. Opin. Lipidol. 12, 419-423
29. Murase, T., Kume, N., Kataoka, H., Minami, M., Sawamura, T., Masaki, T., and Kita, T. (2000) Identification of soluble forms of lectin-like oxidized LDL receptor-1. Arterioscler. Thromb Vasc. Biol. 20, 715-720
30. Cooper, T.M. and Woody, R.W. (1990) The effect of conformation on the CD of interacting helices: a theoretical study of tropomyosin. Biopolymers 30, 657-676
31. Zhou, N.E., Kay, C.M., and Hodges, R.S. (1992) Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils. J. Biol. Chem. 267, 2664-2670
32. Kammerer, R.A., Schulthess, T., Landwehr, R., Lustig, A., Engel, J., Aebi, U., and Steinmetz, M.O. (1998) An autonomous folding unit mediates the assembly of two-stranded coiled coils. Proc. Natl. Acad. Sci. USA 95, 13419-13424
33. Bain, A.D. (2003) Chemical exchange in NMR. Prog. Nucl. Magn. Reson. Spectrosc. 43, 63-103
34. McLachlan, A.D. and Stewart, M. (1975) Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98, 293-304
35. Sodek, J., Dges, R.S.H., Smillie, L.B., and Jurasek, L. (1972) Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc. Natl. Acad. Sci. USA 69, 3800-3804
36. Kohn, W.D., Mant, C.T., and Hodges, R.S. (1997) Alphahelical protein assembly motifs. J. Biol. Chem. 272, 2583-2586
37. Li, Y., Brown, J.H., Reshetnikova, L., Blazsek, A., Farkas, L., Nyitray, L., and Cohen, C. (2003) Visualization of an unstable coiled coil from the scallop myosin rod. Nature 424, 341-345
38. Li, Y., Mui, S., Brown, J.H., Strand, J., Reshetnikova, L., Tobacman, L.S., and Cohen, C. (2002) The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site. Proc. Natl. Acad. Sci. USA 99, 7378-7383
39. Steinmetz, M.O., Stock, A., Schulthess, T., Landwehr, R., Lustig, A., Faix, J., Gerisch, G., Aebi, U., and Kammerer, R.A. (1998) A distinct 14 residue site triggers coiled-coil formation in cortexillin I. EMBO J. 17, 1883-1891
40. Segrest, J.P., Jones, M.K., De Loof, H., and Dashti, N. (2001) Structure of apolipoprotein B-100 in low density lipoproteins. J. Lipid Res. 42, 1346-1367
41. De Loof, H., Rosseneu, M., Yang, C.Y., Li, W.H., Gotto, A.M., and Chan, L. (1987) Human apolipoprotein B: analysis of internal repeats and homology with other apolipoproteins. J. Lipid Res. 28, 1455-1465
42. Lauzon, A.M., Fagnant, P.M., Warshaw, D.M., and Trybus, K.M. (2001) Coiled-coil unwinding at the smooth muscle myosin head-rod junction is required for optimal mechanical performance. Biophys. J. 80, 1900-1904
43. Cambi, A., de Lange, F., van Maarseveen, N.M., Nijhuis, M., Joosten, B., van Dijk, E.M., de Bakker, B.I., Fransen, J.A., Bovee-Geurts, P.H., van Leeuwen, F.N., Van Hulst, N.F., and Figdor, C.G. (2004) Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells. J. Cell Biol. 164, 145-155