메뉴 건너뛰기




Volumn 369, Issue 3, 2007, Pages 784-793

The Structure of OMCI, a Novel Lipocalin Inhibitor of the Complement System

Author keywords

complement C5; complement inhibitor; lipocalin; OmCI; tick

Indexed keywords

CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT COMPONENT C5 INHIBITOR; COMPLEMENT COMPONENT C5A; FATTY ACID DERIVATIVE; LIPOCALIN; PROTEIN; PROTEIN INHIBITOR; PROTEIN OMCI; RICINOLEIC ACID; UNCLASSIFIED DRUG;

EID: 34248165965     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.03.064     Document Type: Article
Times cited : (46)

References (57)
  • 1
    • 0024150429 scopus 로고
    • Structure, organization, and regulation of the complement genes
    • Campbell R.D., Law S.K., Reid K.B., and Sim R.B. Structure, organization, and regulation of the complement genes. Annu. Rev. Immunol. 6 (1988) 161-195
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 161-195
    • Campbell, R.D.1    Law, S.K.2    Reid, K.B.3    Sim, R.B.4
  • 2
    • 0001754187 scopus 로고    scopus 로고
    • Characterization of complement anaphylatoxins and their biological responses
    • Volanakis J.E., et al. (Ed), Marcel Dekker, New York
    • Ember J.A.a.J., and Mark A. Characterization of complement anaphylatoxins and their biological responses. In: Volanakis J.E., et al. (Ed). The Human Complement System in Health and Disease (1998), Marcel Dekker, New York 241
    • (1998) The Human Complement System in Health and Disease , pp. 241
    • Ember, J.A.a.J.1    Mark, A.2
  • 3
    • 0034861323 scopus 로고    scopus 로고
    • Anaphylatoxins and infectious and non-infectious inflammatory diseases
    • Kohl J. Anaphylatoxins and infectious and non-infectious inflammatory diseases. Mol. Immunol. 38 (2001) 175-187
    • (2001) Mol. Immunol. , vol.38 , pp. 175-187
    • Kohl, J.1
  • 4
    • 0033921989 scopus 로고    scopus 로고
    • Complement inhibitors: a resurgent concept in anti-inflammatory therapeutics
    • Sahu A., and Lambris J.D. Complement inhibitors: a resurgent concept in anti-inflammatory therapeutics. Immunopharmacology 49 (2000) 133-148
    • (2000) Immunopharmacology , vol.49 , pp. 133-148
    • Sahu, A.1    Lambris, J.D.2
  • 5
    • 0035369621 scopus 로고    scopus 로고
    • Structure of complement receptor 2 in complex with its C3d ligand
    • Szakonyi G., Guthridge J.M., Li D., Young K., Holers V.M., and Chen X.S. Structure of complement receptor 2 in complex with its C3d ligand. Science 292 (2001) 1725-1728
    • (2001) Science , vol.292 , pp. 1725-1728
    • Szakonyi, G.1    Guthridge, J.M.2    Li, D.3    Young, K.4    Holers, V.M.5    Chen, X.S.6
  • 6
    • 2942536153 scopus 로고    scopus 로고
    • The electrostatic nature of C3d-complement receptor 2 association
    • Morikis D., and Lambris J.D. The electrostatic nature of C3d-complement receptor 2 association. J. Immunol. 172 (2004) 7537-7547
    • (2004) J. Immunol. , vol.172 , pp. 7537-7547
    • Morikis, D.1    Lambris, J.D.2
  • 9
    • 0035019518 scopus 로고    scopus 로고
    • Complement evasion by Borrelia burgdorferi: serum-resistant strains promote C3b inactivation
    • Alitalo A., Meri T., Ramo L., Jokiranta T.S., Heikkila T., Seppala I.J., et al. Complement evasion by Borrelia burgdorferi: serum-resistant strains promote C3b inactivation. Infect. Immun. 69 (2001) 3685-3691
    • (2001) Infect. Immun. , vol.69 , pp. 3685-3691
    • Alitalo, A.1    Meri, T.2    Ramo, L.3    Jokiranta, T.S.4    Heikkila, T.5    Seppala, I.J.6
  • 10
    • 0036841294 scopus 로고    scopus 로고
    • Acquisition of regulators of complement activation by Streptococcus pyogenes serotype M1
    • Pandiripally V., Gregory E., and Cue D. Acquisition of regulators of complement activation by Streptococcus pyogenes serotype M1. Infect. Immun. 70 (2002) 6206-6214
    • (2002) Infect. Immun. , vol.70 , pp. 6206-6214
    • Pandiripally, V.1    Gregory, E.2    Cue, D.3
  • 11
    • 0034705418 scopus 로고    scopus 로고
    • Purification, cloning, and expression of a novel salivary anticomplement protein from the tick Ixodes scapularis
    • Valenzuela J.G., Charlab R., Mather T.N., and Ribeiro J.M. Purification, cloning, and expression of a novel salivary anticomplement protein from the tick Ixodes scapularis. J. Biol. Chem. 275 (2000) 18717-18723
    • (2000) J. Biol. Chem. , vol.275 , pp. 18717-18723
    • Valenzuela, J.G.1    Charlab, R.2    Mather, T.N.3    Ribeiro, J.M.4
  • 12
    • 0022795651 scopus 로고
    • Ixodes dammini: salivary anaphylatoxin inactivating activity
    • Ribeiro J.M., and Spielman A. Ixodes dammini: salivary anaphylatoxin inactivating activity. Expt. Parasitol. 62 (1986) 292-297
    • (1986) Expt. Parasitol. , vol.62 , pp. 292-297
    • Ribeiro, J.M.1    Spielman, A.2
  • 14
    • 0033040796 scopus 로고    scopus 로고
    • Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure
    • Paesen G.C., Adams P.L., Harlos K., Nuttall P.A., and Stuart D.I. Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure. Mol. Cell 3 (1999) 661-671
    • (1999) Mol. Cell , vol.3 , pp. 661-671
    • Paesen, G.C.1    Adams, P.L.2    Harlos, K.3    Nuttall, P.A.4    Stuart, D.I.5
  • 15
    • 0037743752 scopus 로고    scopus 로고
    • The major tick salivary gland proteins and toxins from the soft tick, Ornithodoros savignyi, are part of the tick Lipocalin family: implications for the origins of tick toxicoses
    • Mans B.J., Louw A.I., and Neitz A.W. The major tick salivary gland proteins and toxins from the soft tick, Ornithodoros savignyi, are part of the tick Lipocalin family: implications for the origins of tick toxicoses. Mol. Biol. Evol. 20 (2003) 1158-1167
    • (2003) Mol. Biol. Evol. , vol.20 , pp. 1158-1167
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.3
  • 16
    • 14044268137 scopus 로고    scopus 로고
    • The staphylococcal superantigen-like protein 7 binds IgA and complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria
    • Langley R., Wines B., Willoughby N., Basu I., Proft T., and Fraser J.D. The staphylococcal superantigen-like protein 7 binds IgA and complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria. J. Immunol. 174 (2005) 2926-2933
    • (2005) J. Immunol. , vol.174 , pp. 2926-2933
    • Langley, R.1    Wines, B.2    Willoughby, N.3    Basu, I.4    Proft, T.5    Fraser, J.D.6
  • 18
    • 0032557324 scopus 로고    scopus 로고
    • X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2
    • Nagar B., Jones R.G., Diefenbach R.J., Isenman D.E., and Rini J.M. X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2. Science 280 (1998) 1277-1281
    • (1998) Science , vol.280 , pp. 1277-1281
    • Nagar, B.1    Jones, R.G.2    Diefenbach, R.J.3    Isenman, D.E.4    Rini, J.M.5
  • 20
    • 25644452794 scopus 로고    scopus 로고
    • Structures of complement component C3 provide insights into the function and evolution of immunity
    • Janssen B.J., Huizinga E.G., Raaijmakers H.C., Roos A., Daha M.R., Nilsson-Ekdahl K., et al. Structures of complement component C3 provide insights into the function and evolution of immunity. Nature 437 (2005) 505-511
    • (2005) Nature , vol.437 , pp. 505-511
    • Janssen, B.J.1    Huizinga, E.G.2    Raaijmakers, H.C.3    Roos, A.4    Daha, M.R.5    Nilsson-Ekdahl, K.6
  • 21
    • 33750859976 scopus 로고    scopus 로고
    • Structure of C3b reveals conformational changes that underlie complement activity
    • Janssen B.J., Christodoulidou A., McCarthy A., Lambris J.D., and Gros P. Structure of C3b reveals conformational changes that underlie complement activity. Nature 444 (2006) 213-216
    • (2006) Nature , vol.444 , pp. 213-216
    • Janssen, B.J.1    Christodoulidou, A.2    McCarthy, A.3    Lambris, J.D.4    Gros, P.5
  • 22
    • 33750873601 scopus 로고    scopus 로고
    • Structure of C3b in complex with CRIg gives insights into regulation of complement activation
    • Wiesmann C., Katschke K.J., Yin J., Helmy K.Y., Steffek M., Fairbrother W.J., et al. Structure of C3b in complex with CRIg gives insights into regulation of complement activation. Nature 444 (2006) 217-220
    • (2006) Nature , vol.444 , pp. 217-220
    • Wiesmann, C.1    Katschke, K.J.2    Yin, J.3    Helmy, K.Y.4    Steffek, M.5    Fairbrother, W.J.6
  • 24
    • 0024493978 scopus 로고
    • Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance data
    • Zuiderweg E.R., Nettesheim D.G., Mollison K.W., and Carter G.W. Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance data. Biochemistry 28 (1989) 172-185
    • (1989) Biochemistry , vol.28 , pp. 172-185
    • Zuiderweg, E.R.1    Nettesheim, D.G.2    Mollison, K.W.3    Carter, G.W.4
  • 25
    • 0030999525 scopus 로고    scopus 로고
    • Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy
    • Zhang X., Boyar W., Toth M.J., Wennogle L., and Gonnella N.C. Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy. Proteins: Struct. Funct. Genet. 28 (1997) 261-267
    • (1997) Proteins: Struct. Funct. Genet. , vol.28 , pp. 261-267
    • Zhang, X.1    Boyar, W.2    Toth, M.J.3    Wennogle, L.4    Gonnella, N.C.5
  • 26
    • 15444371872 scopus 로고    scopus 로고
    • Functional insights from the structure of the multifunctional C345C domain of C5 of complement
    • Bramham J., Thai C.T., Soares D.C., Uhrin D., Ogata R.T., and Barlow P.N. Functional insights from the structure of the multifunctional C345C domain of C5 of complement. J. Biol. Chem. 280 (2005) 10636-10645
    • (2005) J. Biol. Chem. , vol.280 , pp. 10636-10645
    • Bramham, J.1    Thai, C.T.2    Soares, D.C.3    Uhrin, D.4    Ogata, R.T.5    Barlow, P.N.6
  • 27
    • 0345735840 scopus 로고    scopus 로고
    • Expression and characterization of the C345C/NTR domains of complement components C3 and C5
    • Thai C.T., and Ogata R.T. Expression and characterization of the C345C/NTR domains of complement components C3 and C5. J. Immunol. 171 (2003) 6565-6573
    • (2003) J. Immunol. , vol.171 , pp. 6565-6573
    • Thai, C.T.1    Ogata, R.T.2
  • 28
    • 4644327017 scopus 로고    scopus 로고
    • Complement components C5 and C7: recombinant factor I modules of C7 bind to the C345C domain of C5
    • Thai C.T., and Ogata R.T. Complement components C5 and C7: recombinant factor I modules of C7 bind to the C345C domain of C5. J. Immunol. 173 (2004) 4547-4552
    • (2004) J. Immunol. , vol.173 , pp. 4547-4552
    • Thai, C.T.1    Ogata, R.T.2
  • 29
    • 0034661670 scopus 로고    scopus 로고
    • Distal recognition site for classical pathway convertase located in the C345C/netrin module of complement component C5
    • Sandoval A., Ai R., Ostresh J.M., and Ogata R.T. Distal recognition site for classical pathway convertase located in the C345C/netrin module of complement component C5. J. Immunol. 165 (2000) 1066-1073
    • (2000) J. Immunol. , vol.165 , pp. 1066-1073
    • Sandoval, A.1    Ai, R.2    Ostresh, J.M.3    Ogata, R.T.4
  • 31
    • 29744436872 scopus 로고    scopus 로고
    • Eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria
    • Hill A. Eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria. Clin. Advan. Hematol. Oncol. 3 (2005) 849-850
    • (2005) Clin. Advan. Hematol. Oncol. , vol.3 , pp. 849-850
    • Hill, A.1
  • 33
    • 31044431837 scopus 로고    scopus 로고
    • Inhibition of complement activation in cardiac surgery
    • Sellke F.W., and Boodhwani M. Inhibition of complement activation in cardiac surgery. J. Thorac. Cardiovasc. Surg. 131 (2006) 266-267
    • (2006) J. Thorac. Cardiovasc. Surg. , vol.131 , pp. 266-267
    • Sellke, F.W.1    Boodhwani, M.2
  • 34
    • 2942716917 scopus 로고    scopus 로고
    • Inhibition of terminal complement: a novel therapeutic approach for the treatment of systemic lupus erythematosus
    • Rother R.P., Mojcik C.F., and McCroskery E.W. Inhibition of terminal complement: a novel therapeutic approach for the treatment of systemic lupus erythematosus. Lupus 13 (2004) 328-334
    • (2004) Lupus , vol.13 , pp. 328-334
    • Rother, R.P.1    Mojcik, C.F.2    McCroskery, E.W.3
  • 36
    • 0034684234 scopus 로고    scopus 로고
    • Tick histamine-binding proteins: lipocalins with a second binding cavity
    • Paesen G.C., Adams P.L., Nuttall P.A., and Stuart D.L. Tick histamine-binding proteins: lipocalins with a second binding cavity. Biochim. Biophys. Acta 1482 (2000) 92-101
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 92-101
    • Paesen, G.C.1    Adams, P.L.2    Nuttall, P.A.3    Stuart, D.L.4
  • 37
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • Lee B., and Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55 (1971) 379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 38
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L., and Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 39
    • 57649133146 scopus 로고    scopus 로고
    • Identification of putative proteins involved in granule biogenesis of tick salivary glands
    • Mans B.J., Venter J.D., Vrey P.J., Louw A.I., and Neitz A.W. Identification of putative proteins involved in granule biogenesis of tick salivary glands. Electrophoresis 22 (2001) 1739-1746
    • (2001) Electrophoresis , vol.22 , pp. 1739-1746
    • Mans, B.J.1    Venter, J.D.2    Vrey, P.J.3    Louw, A.I.4    Neitz, A.W.5
  • 40
    • 0027418305 scopus 로고
    • Isolation of an inhibitor selective for collagen-stimulated platelet aggregation from the soft tick Ornithodoros moubata
    • Waxman L., and Connolly T.M. Isolation of an inhibitor selective for collagen-stimulated platelet aggregation from the soft tick Ornithodoros moubata. J. Biol. Chem. 268 (1993) 5445-5549
    • (1993) J. Biol. Chem. , vol.268 , pp. 5445-5549
    • Waxman, L.1    Connolly, T.M.2
  • 41
    • 14844331097 scopus 로고    scopus 로고
    • IgE-mediated anaphylaxis caused by bites of the pigeon tick Argas reflexus: cloning and expression of the major allergen Arg r 1
    • Hilger C., Bessot J.C., Hutt N., Grigioni F., De Blay F., Pauli G., and Hentges F. IgE-mediated anaphylaxis caused by bites of the pigeon tick Argas reflexus: cloning and expression of the major allergen Arg r 1. J. Allergy Clin. Immunol. 115 (2005) 617-622
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 617-622
    • Hilger, C.1    Bessot, J.C.2    Hutt, N.3    Grigioni, F.4    De Blay, F.5    Pauli, G.6    Hentges, F.7
  • 43
    • 0036843632 scopus 로고    scopus 로고
    • Role of the human C8 subunits in complement-mediated bacterial killing: evidence that C8 gamma is not essential
    • Parker C.L., and Sodetz J.M. Role of the human C8 subunits in complement-mediated bacterial killing: evidence that C8 gamma is not essential. Mol. Immuno. 39 (2002) 453-458
    • (2002) Mol. Immuno. , vol.39 , pp. 453-458
    • Parker, C.L.1    Sodetz, J.M.2
  • 44
    • 0037018929 scopus 로고    scopus 로고
    • Crystal structure of human complement protein C8gamma at 1.2 Å resolution reveals a lipocalin fold and a distinct ligand binding site
    • Ortlund E., Parker C.L., Schreck S.F., Ginell S., Minor W., Sodetz J.M., and Lebioda L. Crystal structure of human complement protein C8gamma at 1.2 Å resolution reveals a lipocalin fold and a distinct ligand binding site. Biochemistry 41 (2002) 7030-7037
    • (2002) Biochemistry , vol.41 , pp. 7030-7037
    • Ortlund, E.1    Parker, C.L.2    Schreck, S.F.3    Ginell, S.4    Minor, W.5    Sodetz, J.M.6    Lebioda, L.7
  • 45
    • 33646195686 scopus 로고    scopus 로고
    • Detection of protein assemblies in crystals
    • Berthold M.R. (Ed), Springer, Berlin
    • Krissinel E.A.H.K. Detection of protein assemblies in crystals. In: Berthold M.R. (Ed). Lecture Notes in Computer Science vol. 3695 (2005), Springer, Berlin 163-174
    • (2005) Lecture Notes in Computer Science , vol.3695 , pp. 163-174
    • Krissinel, E.A.H.K.1
  • 46
    • 0037134011 scopus 로고    scopus 로고
    • Role of prostacyclin in the cardiovascular response to thromboxane A2
    • Cheng Y., Austin S.C., Rocca B., Koller B.H., Coffman T.M., Grosser T., et al. Role of prostacyclin in the cardiovascular response to thromboxane A2. Science 296 (2002) 539-541
    • (2002) Science , vol.296 , pp. 539-541
    • Cheng, Y.1    Austin, S.C.2    Rocca, B.3    Koller, B.H.4    Coffman, T.M.5    Grosser, T.6
  • 47
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallog. sect. D 62 (2006) 48-57
    • (2006) Acta Crystallog. sect. D , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 48
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P. Scaling and assessment of data quality. Acta Crystallog. sect. D 62 (2006) 72-82
    • (2006) Acta Crystallog. sect. D , vol.62 , pp. 72-82
    • Evans, P.1
  • 49
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog 50 (1994) 157-163
    • (1994) Acta Crystallog , vol.50 , pp. 157-163
    • Navaza, J.1
  • 50
  • 51
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 53
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 55
    • 0024267619 scopus 로고
    • Amino acid substitutions in structurally related proteins. A pattern recognition approach. Determination of a new and efficient scoring matrix
    • Risler J.L., Delorme M.O., Delacroix H., and Henaut A. Amino acid substitutions in structurally related proteins. A pattern recognition approach. Determination of a new and efficient scoring matrix. J. Mol. Biol. 204 (1988) 1019-1029
    • (1988) J. Mol. Biol. , vol.204 , pp. 1019-1029
    • Risler, J.L.1    Delorme, M.O.2    Delacroix, H.3    Henaut, A.4
  • 56
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P., Robert X., and Courcelle E. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucl. Acids Res. 31 (2003) 3320-3323
    • (2003) Nucl. Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 57
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8 (1995) 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.