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Volumn 500, Issue 7461, 2013, Pages 227-231

Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84881479703     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12328     Document Type: Article
Times cited : (588)

References (38)
  • 2
    • 84867733836 scopus 로고    scopus 로고
    • Severe respiratory illness caused by a novel coronavirus, in a patient transferred to theUnited Kingdomfromthe Middle East, September2012
    • 20290
    • Bermingham, A. et al. Severe respiratory illness caused by a novel coronavirus, in a patient transferred to theUnited Kingdomfromthe Middle East, September2012. Euro Surveill. 17, 20290 (2012).
    • (2012) Euro Surveill , vol.17
    • Bermingham, A.1
  • 4
    • 84874996988 scopus 로고    scopus 로고
    • Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
    • Raj, V. S. et al. Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 495, 251-254 (2013).
    • (2013) Nature , vol.495 , pp. 251-254
    • Raj, V.S.1
  • 5
    • 84865302785 scopus 로고    scopus 로고
    • Novel coronavirus infection - update
    • World Health Organization. Novel coronavirus infection - update. http://www.who.int/csr/don/2013-05-15-ncov/en/(2013).
    • (2013) World Health Organization
  • 6
    • 29144451985 scopus 로고    scopus 로고
    • Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus
    • Weiss, S. R. & Navas-Martin, S. Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus. Microbiol. Mol. Biol. Rev. 69, 635-664 (2005).
    • (2005) Microbiol. Mol. Biol. Rev , vol.69 , pp. 635-664
    • Weiss, S.R.1    Navas-Martin, S.2
  • 7
    • 84871415482 scopus 로고    scopus 로고
    • Genomic characterization of a newly discovered coronavirus associated with acute respiratory distress syndrome in humans
    • van Boheemen, S. et al. Genomic characterization of a newly discovered coronavirus associated with acute respiratory distress syndrome in humans.mBio 3, e00473-e12 (2012).
    • (2012) Bio , vol.3
    • Van Boheemen, S.1
  • 8
    • 84869035188 scopus 로고    scopus 로고
    • SARS-like virus in the Middle East: A truly bat-related coronavirus causing human diseases
    • Lu, G. & Liu, D. SARS-like virus in the Middle East: a truly bat-related coronavirus causing human diseases. Protein Cell 3, 803-805 (2012).
    • (2012) Protein Cell , vol.3 , pp. 803-805
    • Lu, G.1    Liu, D.2
  • 9
    • 84872146295 scopus 로고    scopus 로고
    • Humancoronavirus EMCdoes not require the SARS-coronavirus receptor andmaintains broad replicative capability inmammalian cell lines
    • Müller, M. A. et al.Humancoronavirus EMCdoes not require the SARS-coronavirus receptor andmaintains broad replicative capability inmammalian cell lines. mBio 3, e00515-e12 (2012).
    • (2012) Bio , vol.3
    • Müller, M.A.1
  • 10
    • 0026693135 scopus 로고
    • Human aminopeptidase N is a receptor for human coronavirus 229E
    • Yeager, C. L. et al. Human aminopeptidase N is a receptor for human coronavirus 229E. Nature 357, 420-422 (1992).
    • (1992) Nature , vol.357 , pp. 420-422
    • Yeager, C.L.1
  • 11
    • 0026729302 scopus 로고
    • Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV
    • Delmas, B. et al. Aminopeptidase N is a major receptor for the entero-pathogenic coronavirus TGEV. Nature 357, 417-420 (1992).
    • (1992) Nature , vol.357 , pp. 417-420
    • Delmas, B.1
  • 12
    • 0344395657 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
    • Li, W. et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426, 450-454 (2003).
    • (2003) Nature , vol.426 , pp. 450-454
    • Li, W.1
  • 14
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel, J. J. & Wiley, D. C. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95, 871-874 (1998).
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 15
    • 2442705099 scopus 로고    scopus 로고
    • Following the rule: Formation of the 6-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors
    • Zhu, J. et al. Following the rule: formation of the 6-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors. Biochem. Biophys. Res. Commun. 319, 283-288 (2004).
    • (2004) Biochem. Biophys. Res. Commun , vol.319 , pp. 283-288
    • Zhu, J.1
  • 16
    • 79960567167 scopus 로고    scopus 로고
    • Crystal structure of mouse coronavirus receptor-binding domain complexed with itsmurine receptor
    • Peng,G. et al. Crystal structure of mouse coronavirus receptor-binding domain complexed with itsmurine receptor. Proc.NatlAcad. Sci.USA108, 10696-10701(2011).
    • (2011) Proc.NatlAcad. Sci.USA108 , pp. 10696-10701
    • Peng, G.1
  • 17
    • 24944498409 scopus 로고    scopus 로고
    • Structure ofSARScoronavirusspikereceptorbinding domain complexed with receptor
    • Li, F., Li,W.,Farzan,M.&Harrison,S.C.Structure ofSARScoronavirusspikereceptorbinding domain complexed with receptor. Science 309, 1864-1868 (2005).
    • (2005) Science , vol.309 , pp. 1864-1868
    • Li, F.1    Li, W.2    Farzan, M.3    Harrison, S.C.4
  • 18
    • 73949110051 scopus 로고    scopus 로고
    • Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor
    • Wu, K., Li, W., Peng, G. & Li, F. Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor. Proc. Natl Acad. Sci. USA 106, 19970-19974 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 19970-19974
    • Wu, K.1    Li, W.2    Peng, G.3    Li, F.4
  • 19
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. & Rosenstrom, P. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549 (2010).
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 20
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • Rasmussen, H. B., Branner, S., Wiberg, F. C. & Wagtmann, N. Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nature Struct. Biol. 10, 19-25 (2003).
    • (2003) Nature Struct. Biol , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4
  • 21
    • 0037966007 scopus 로고    scopus 로고
    • The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism
    • Engel, M. et al. The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proc. Natl Acad. Sci. USA 100, 5063-5068 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5063-5068
    • Engel, M.1
  • 22
    • 0035723325 scopus 로고    scopus 로고
    • CD26: A multifunctional integral membrane and secreted protein of activated lymphocytes
    • Gorrell, M. D., Gysbers, V. & McCaughan, G. W. CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes. Scand. J. Immunol. 54, 249-264 (2001).
    • (2001) Scand. J. Immunol , vol.54 , pp. 249-264
    • Gorrell, M.D.1    Gysbers, V.2    McCaughan, G.W.3
  • 23
    • 5644261220 scopus 로고    scopus 로고
    • Crystal structure ofCD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface
    • Weihofen, W. A., Liu, J., Reutter, W., Saenger, W.&Fan, H. Crystal structure ofCD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface. J. Biol. Chem. 279, 43330-43335 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 43330-43335
    • Weihofen, W.A.1    Liu, J.2    Reutter, W.3    Saenger, W.4    Fan, H.5
  • 24
    • 35648986721 scopus 로고    scopus 로고
    • ed. Knipe, D.M., Lippincott Williams & Wilkins
    • Lai, M. M., Perlman, S. & Anderson, L. J. in Fields Virology (ed. Knipe, D.M.) 1305-1336 (Lippincott Williams & Wilkins, 2007).
    • (2007) Fields Virology , pp. 1305-1336
    • Lai, M.M.1    Perlman, S.2    Anderson, L.J.3
  • 25
    • 84866168715 scopus 로고    scopus 로고
    • Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies
    • Reguera, J. et al. Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies. PLoS Pathog. 8, e1002859 (2012).
    • (2012) PLoS Pathog , vol.8
    • Reguera, J.1
  • 26
    • 84857809414 scopus 로고    scopus 로고
    • Evidence for a common evolutionary origin of coronavirus spike protein receptor-binding subunits
    • Li, F. Evidence for a common evolutionary origin of coronavirus spike protein receptor-binding subunits. J. Virol. 86, 2856-2858 (2012).
    • (2012) J. Virol , vol.86 , pp. 2856-2858
    • Li, F.1
  • 28
    • 84877339392 scopus 로고    scopus 로고
    • The spike-protein of the emerging betacoronavirus EMC uses a novel coronavirus receptor for entry, canbeactivated byTMPRSS2,and is targeted by neutralizing antibodies
    • Gierer, S. et al. The spike-protein of the emerging betacoronavirus EMC uses a novel coronavirus receptor for entry, canbeactivated byTMPRSS2,and is targeted by neutralizing antibodies. J. Virol. 87, 5502-5511 (2013).
    • (2013) J. Virol , vol.87 , pp. 5502-5511
    • Gierer, S.1
  • 29
    • 77957816428 scopus 로고    scopus 로고
    • Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918pandemic virus
    • Zhang, W. et al. Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918pandemic virus. Protein Cell 1, 459-467 (2010).
    • (2010) Protein Cell , vol.1 , pp. 459-467
    • Zhang, W.1
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0028103275 scopus 로고
    • Collaborative Computing ProjectNumber 4. The CCP4 suite: Programsfor protein crystallography
    • Collaborative Computing ProjectNumber 4. The CCP4 suite: programsfor protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr , vol.50 , pp. 760-763
  • 32
    • 0038210935 scopus 로고    scopus 로고
    • Advances in direct methods for protein crystallography
    • Usó n, I. & Sheldrick, G. M. Advances in direct methods for protein crystallography. Curr. Opin. Struct. Biol. 9, 643-648 (1999).
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 643-648
    • Uson, I.1    Sheldrick, G.M.2
  • 33
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R. J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr. D 57, 1373-1382 (2001).
    • (2001) Acta Crystallogr D , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 34
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan, K. D. & Zhang, K. Y. Density modification for macromolecular phase improvement. Prog. Biophys. Mol. Biol. 72, 245-270 (1999).
    • (1999) Prog. Biophys. Mol. Biol , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 35
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 36
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr , vol.D 60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 37
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 38
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D. I. & Metoz, F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308 (1999).
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


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