메뉴 건너뛰기




Volumn 8, Issue 12, 2012, Pages

The Two Sides of Complement C3d: Evolution of Electrostatics in a Link between Innate and Adaptive Immunity

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; ELECTROSTATICS; IMMUNE SYSTEM; MOLECULAR DYNAMICS;

EID: 84872017201     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002840     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 33947126628 scopus 로고    scopus 로고
    • Complement-mediated activation of the adaptive immune responses
    • Toapanta F, Ross T, (2006) Complement-mediated activation of the adaptive immune responses. Immunol Res 36: 197-210.
    • (2006) Immunol Res , vol.36 , pp. 197-210
    • Toapanta, F.1    Ross, T.2
  • 2
    • 0035006284 scopus 로고    scopus 로고
    • Structure and biology of complement protein C3, a connecting link between innate and acquired immunity
    • Sahu A, Lambris J, (2001) Structure and biology of complement protein C3, a connecting link between innate and acquired immunity. Immunol Rev 180: 35-48.
    • (2001) Immunol Rev , vol.180 , pp. 35-48
    • Sahu, A.1    Lambris, J.2
  • 3
    • 5444259851 scopus 로고    scopus 로고
    • The complement system in regulation of adaptive immunity
    • doi:10.1038/ni1113
    • Carroll MC, (2004) The complement system in regulation of adaptive immunity. Nat Immunol 5: 981-986 doi:10.1038/ni1113.
    • (2004) Nat Immunol , vol.5 , pp. 981-986
    • Carroll, M.C.1
  • 4
    • 0043011079 scopus 로고    scopus 로고
    • Evolution of complement as an effector system in innate and adaptive immunity
    • Sunyer J, Boshra H, Lorenzo G, Parra D, Freedman B, et al. (2003) Evolution of complement as an effector system in innate and adaptive immunity. Immunol Res 27: 549-564.
    • (2003) Immunol Res , vol.27 , pp. 549-564
    • Sunyer, J.1    Boshra, H.2    Lorenzo, G.3    Parra, D.4    Freedman, B.5
  • 5
    • 78549235728 scopus 로고    scopus 로고
    • Delineation of the complement receptor type 2-C3d complex by site-directed mutagenesis and molecular docking
    • doi:10.1016/j.jmb.2010.10.005
    • Shaw CD, Storek MJ, Young KA, Kovacs JM, Thurman JM, et al. (2010) Delineation of the complement receptor type 2-C3d complex by site-directed mutagenesis and molecular docking. J Mol Biol 404: 697-710 doi:10.1016/j.jmb.2010.10.005.
    • (2010) J Mol Biol , vol.404 , pp. 697-710
    • Shaw, C.D.1    Storek, M.J.2    Young, K.A.3    Kovacs, J.M.4    Thurman, J.M.5
  • 6
    • 66149096224 scopus 로고    scopus 로고
    • Mapping of the C3d ligand binding site on complement receptor 2 (CR2/CD21) using nuclear magnetic resonance and chemical shift analysis
    • doi:10.1074/jbc.M808404200
    • Kovacs JM, Hannan JP, Eisenmesser EZ, Holers VM, (2009) Mapping of the C3d ligand binding site on complement receptor 2 (CR2/CD21) using nuclear magnetic resonance and chemical shift analysis. J Biol Chem 284: 9513-9520 doi:10.1074/jbc.M808404200.
    • (2009) J Biol Chem , vol.284 , pp. 9513-9520
    • Kovacs, J.M.1    Hannan, J.P.2    Eisenmesser, E.Z.3    Holers, V.M.4
  • 7
    • 13844255020 scopus 로고    scopus 로고
    • Mutational analysis of the complement receptor type 2 (CR2/CD21)-C3d interaction reveals a putative charged SCR1 binding site for C3d
    • Hannan J, Young K, Guthridge J, Asokan R, Szakonyi G, et al. (2005) Mutational analysis of the complement receptor type 2 (CR2/CD21)-C3d interaction reveals a putative charged SCR1 binding site for C3d. J Mol Biol 346: 845-858.
    • (2005) J Mol Biol , vol.346 , pp. 845-858
    • Hannan, J.1    Young, K.2    Guthridge, J.3    Asokan, R.4    Szakonyi, G.5
  • 8
    • 0034292433 scopus 로고    scopus 로고
    • Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21)
    • Clemenza L, Isenman D, (2000) Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21). J Immunol 165: 3839-3848.
    • (2000) J Immunol , vol.165 , pp. 3839-3848
    • Clemenza, L.1    Isenman, D.2
  • 9
    • 54249162843 scopus 로고    scopus 로고
    • Solution structure of the complex formed between human complement C3d and full-length complement receptor type 2
    • doi:10.1016/j.jmb.2008.08.084
    • Li K, Okemefuna AI, Gor J, Hannan JP, Asokan R, et al. (2008) Solution structure of the complex formed between human complement C3d and full-length complement receptor type 2. J Mol Biol 384: 137-150 doi:10.1016/j.jmb.2008.08.084.
    • (2008) J Mol Biol , vol.384 , pp. 137-150
    • Li, K.1    Okemefuna, A.I.2    Gor, J.3    Hannan, J.P.4    Asokan, R.5
  • 10
    • 0032557324 scopus 로고    scopus 로고
    • X-ray crystal structure of C3d: A C3 fragment and ligand for complement receptor 2
    • Nagar B, Jones R, Diefenbach R, Isenman D, Rini J, (1998) X-ray crystal structure of C3d: A C3 fragment and ligand for complement receptor 2. Science 280: 1277-1281.
    • (1998) Science , vol.280 , pp. 1277-1281
    • Nagar, B.1    Jones, R.2    Diefenbach, R.3    Isenman, D.4    Rini, J.5
  • 11
    • 2942536153 scopus 로고    scopus 로고
    • The electrostatic nature of C3d-Complement receptor 2 association
    • Morikis D, Lambris J, (2004) The electrostatic nature of C3d-Complement receptor 2 association. J Immunol 172: 7537-7547.
    • (2004) J Immunol , vol.172 , pp. 7537-7547
    • Morikis, D.1    Lambris, J.2
  • 12
    • 34247617750 scopus 로고    scopus 로고
    • Immunophysical exploration of C3d-CR2(CCP1-2) interaction using molecular dynamics and electrostatics
    • doi:10.1016/j.jmb.2007.02.101
    • Zhang L, Mallik B, Morikis D, (2007) Immunophysical exploration of C3d-CR2(CCP1-2) interaction using molecular dynamics and electrostatics. J Mol Biol 369: 567-583 doi:10.1016/j.jmb.2007.02.101.
    • (2007) J Mol Biol , vol.369 , pp. 567-583
    • Zhang, L.1    Mallik, B.2    Morikis, D.3
  • 13
    • 0030593030 scopus 로고    scopus 로고
    • C3d of complement as a molecular adjuvant: Bridging innate and acquired immunity
    • Dempsey P, Allison M, Akkaraju S, Goodnow C, Fearon D, (1996) C3d of complement as a molecular adjuvant: Bridging innate and acquired immunity. Science 271: 348-350.
    • (1996) Science , vol.271 , pp. 348-350
    • Dempsey, P.1    Allison, M.2    Akkaraju, S.3    Goodnow, C.4    Fearon, D.5
  • 14
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • doi:10.1126/science.7529940
    • Clackson T, Wells J, (1995) A hot spot of binding energy in a hormone-receptor interface. Science 267: 383-386 doi:10.1126/science.7529940.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.2
  • 15
    • 0037609791 scopus 로고    scopus 로고
    • Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces
    • doi:10.1073/pnas.1030237100
    • Ma B, Elkayam T, Wolfson H, Nussinov R, (2003) Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces. P Natl Acad Sci Usa 100: 5772-5777 doi:10.1073/pnas.1030237100.
    • (2003) P Natl Acad Sci Usa , vol.100 , pp. 5772-5777
    • Ma, B.1    Elkayam, T.2    Wolfson, H.3    Nussinov, R.4
  • 16
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B, Nicholls A, (1995) Classical electrostatics in biology and chemistry. Science 268: 1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 17
    • 0034039797 scopus 로고    scopus 로고
    • Electrostatic aspects of protein-protein interactions
    • Sheinerman FB, Norel R, Honig B, (2000) Electrostatic aspects of protein-protein interactions. Curr Opin Struc Biol 10: 153-159.
    • (2000) Curr Opin Struc Biol , vol.10 , pp. 153-159
    • Sheinerman, F.B.1    Norel, R.2    Honig, B.3
  • 18
    • 84857895493 scopus 로고    scopus 로고
    • Complement inhibition by Staphylococcus aureus: Electrostatics of C3d-Efbc and C3d-ehp association
    • Gorham R, Kieslich C, Morikis D, (2011) Complement inhibition by Staphylococcus aureus: Electrostatics of C3d-Efbc and C3d-ehp association. Cell Mol Bioeng 5: 32-43.
    • (2011) Cell Mol Bioeng , vol.5 , pp. 32-43
    • Gorham, R.1    Kieslich, C.2    Morikis, D.3
  • 19
    • 78650607656 scopus 로고    scopus 로고
    • A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d
    • doi:10.1016/j.molimm.2010.09.017
    • Clark EA, Crennell S, Upadhyay A, Zozulya AV, Mackay JD, et al. (2011) A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d. Mol Immunol 48: 452-462 doi:10.1016/j.molimm.2010.09.017.
    • (2011) Mol Immunol , vol.48 , pp. 452-462
    • Clark, E.A.1    Crennell, S.2    Upadhyay, A.3    Zozulya, A.V.4    Mackay, J.D.5
  • 20
    • 77952813339 scopus 로고    scopus 로고
    • Molecular mechanisms of complement evasion: Learning from staphylococci and meningococci
    • doi:10.1038/nrmicro2366
    • Serruto D, Rappuoli R, Scarselli M, Gros P, van Strijp JAG, (2010) Molecular mechanisms of complement evasion: Learning from staphylococci and meningococci. Nat Rev Micro 8: 393-399 doi:10.1038/nrmicro2366.
    • (2010) Nat Rev Micro , vol.8 , pp. 393-399
    • Serruto, D.1    Rappuoli, R.2    Scarselli, M.3    Gros, P.4    van Strijp, J.A.G.5
  • 21
    • 0032568645 scopus 로고    scopus 로고
    • Electrostatic steering and ionic tethering in enzyme-ligand binding: Insights from simulations
    • Wade R, Gabdoulline R, Ludemann S, Lounnas V, (1998) Electrostatic steering and ionic tethering in enzyme-ligand binding: Insights from simulations. Proc Natl Acad Sci USA 95: 5942-5949.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5942-5949
    • Wade, R.1    Gabdoulline, R.2    Ludemann, S.3    Lounnas, V.4
  • 22
  • 23
    • 78751566641 scopus 로고    scopus 로고
    • Is the rigid-body assumption reasonable? Insights into the effects of dynamics on the electrostatic analysis of barnase-barstar
    • doi:10.1016/j.jnoncrysol.2010.05.087
    • Kieslich CA, Gorham RD, Morikis D, (2011) Is the rigid-body assumption reasonable? Insights into the effects of dynamics on the electrostatic analysis of barnase-barstar. J Non-Cryst Solids 357: 707-716 doi:10.1016/j.jnoncrysol.2010.05.087.
    • (2011) J Non-Cryst Solids , vol.357 , pp. 707-716
    • Kieslich, C.A.1    Gorham, R.D.2    Morikis, D.3
  • 24
    • 67349128569 scopus 로고    scopus 로고
    • Dual nature of the adaptive immune system in lampreys
    • doi:10.1038/nature08068
    • Guo P, Hirano M, Herrin BR, Li J, Yu C, et al. (2009) Dual nature of the adaptive immune system in lampreys. Nature 459: 796-802 doi:10.1038/nature08068.
    • (2009) Nature , vol.459 , pp. 796-802
    • Guo, P.1    Hirano, M.2    Herrin, B.R.3    Li, J.4    Yu, C.5
  • 25
    • 66049136648 scopus 로고    scopus 로고
    • Darwinian biophysics: Electrostatics and evolution in the kinetics of molecular binding
    • McCammon J, (2009) Darwinian biophysics: Electrostatics and evolution in the kinetics of molecular binding. Proc Natl Acad Sci USA 106: 7683-7684.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7683-7684
    • McCammon, J.1
  • 26
    • 0000203447 scopus 로고
    • Diffusional dynamics of ligand receptor association
    • McCammon J, Northrup S, Allison S, (1986) Diffusional dynamics of ligand receptor association. J Phys Chem-Us 90: 3901-3905.
    • (1986) J Phys Chem-Us , vol.90 , pp. 3901-3905
    • McCammon, J.1    Northrup, S.2    Allison, S.3
  • 27
    • 0028774340 scopus 로고
    • Stability and function: two constraints in the evolution of barstar and other proteins
    • Schreiber G, Buckle A, Fersht A, (1994) Stability and function: two constraints in the evolution of barstar and other proteins. Structure 2: 945-951.
    • (1994) Structure , vol.2 , pp. 945-951
    • Schreiber, G.1    Buckle, A.2    Fersht, A.3
  • 28
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • UniProt Consortium, doi:10.1093/nar/gkr981
    • UniProt Consortium (2012) Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res 40: D71-D75 doi:10.1093/nar/gkr981.
    • (2012) Nucleic Acids Res , vol.40
  • 29
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • doi:10.1093/nar/gkh340
    • Edgar R, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797 doi:10.1093/nar/gkh340.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.1
  • 30
    • 33750398103 scopus 로고    scopus 로고
    • Bio3d: an R package for the comparative analysis of protein structures
    • doi:10.1093/bioinformatics/btl461
    • Grant BJ, Rodrigues APC, ElSawy KM, McCammon JA, Caves LSD, (2006) Bio3d: an R package for the comparative analysis of protein structures. Bioinformatics 22: 2695-2696 doi:10.1093/bioinformatics/btl461.
    • (2006) Bioinformatics , vol.22 , pp. 2695-2696
    • Grant, B.J.1    Rodrigues, A.P.C.2    ElSawy, K.M.3    McCammon, J.A.4    Caves, L.S.D.5
  • 31
    • 84907095419 scopus 로고    scopus 로고
    • R: A Language and Environment for Statistical Computing
    • R Development Core Team, Available:
    • R Development Core Team (2011) R: A Language and Environment for Statistical Computing. Vienna, Austria. R Foundation for Statistical Computing Available: http://www.R-project.org/.
    • (2011) R Foundation for Statistical Computing
  • 32
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker N, Sept D, Joseph S, Holst M, McCammon J, (2001) Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc Natl Acad Sci USA 98: 10037-10041.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10037-10041
    • Baker, N.1    Sept, D.2    Joseph, S.3    Holst, M.4    McCammon, J.5
  • 33
    • 80052270875 scopus 로고    scopus 로고
    • Calculation of free energy of protein association using Poisson-Boltzmann electrostatics: validation with experimental kinetic data
    • Gorham RD, Kieslich CA, Nichols A, Sausman NU, Foronda M, et al. (2011) Calculation of free energy of protein association using Poisson-Boltzmann electrostatics: validation with experimental kinetic data. Biopolymers 95: 746-54.
    • (2011) Biopolymers , vol.95 , pp. 746-754
    • Gorham, R.D.1    Kieslich, C.A.2    Nichols, A.3    Sausman, N.U.4    Foronda, M.5
  • 34
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • doi:10.1002/jcc.20084
    • Pettersen E, Goddard T, Huang C, Couch G, Greenblatt D, et al. (2004) UCSF Chimera- A visualization system for exploratory research and analysis. J Comput Chem 25: 1605-1612 doi:10.1002/jcc.20084.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.1    Goddard, T.2    Huang, C.3    Couch, G.4    Greenblatt, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.