메뉴 건너뛰기




Volumn 53, Issue 38, 2014, Pages 6084-6091

Long-range stabilization of anthrax protective antigen upon binding to CMG2

Author keywords

[No Author keywords available]

Indexed keywords

PROTECTIVE ANTIGENS;

EID: 84907542501     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500718g     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0026498189 scopus 로고
    • Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin
    • Klimpel, K. R., Molloy, S. S., Thomas, G., and Leppla, S. H. (1992) Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin Proc. Natl. Acad. Sci. U.S.A. 89, 10277-10281
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10277-10281
    • Klimpel, K.R.1    Molloy, S.S.2    Thomas, G.3    Leppla, S.H.4
  • 2
    • 4444267311 scopus 로고    scopus 로고
    • Structure of heptameric protective antigen bound to an anthrax toxin receptor: A role for receptor in pH-dependent pore formation
    • Lacy, D. B., Wigelsworth, D. J., Melnyk, R. A., Harrison, S. C., and Collier, R. J. (2004) Structure of heptameric protective antigen bound to an anthrax toxin receptor: A role for receptor in pH-dependent pore formation Proc. Natl. Acad. Sci. U.S.A. 101, 13147-13151
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13147-13151
    • Lacy, D.B.1    Wigelsworth, D.J.2    Melnyk, R.A.3    Harrison, S.C.4    Collier, R.J.5
  • 4
    • 3542993051 scopus 로고    scopus 로고
    • Crystal structure of a complex between anthrax toxin and its host cell receptor
    • Santelli, E., Bankston, L. A., Leppla, S. H., and Liddington, R. C. (2004) Crystal structure of a complex between anthrax toxin and its host cell receptor Nature 430, 905-908
    • (2004) Nature , vol.430 , pp. 905-908
    • Santelli, E.1    Bankston, L.A.2    Leppla, S.H.3    Liddington, R.C.4
  • 5
    • 0035829509 scopus 로고    scopus 로고
    • Identification of the cellular receptor for anthrax toxin
    • Bradley, K. A., Mogridge, J., Mourez, M., Collier, R. J., and Young, J. A. (2001) Identification of the cellular receptor for anthrax toxin Nature 414, 225-229
    • (2001) Nature , vol.414 , pp. 225-229
    • Bradley, K.A.1    Mogridge, J.2    Mourez, M.3    Collier, R.J.4    Young, J.A.5
  • 6
    • 0033064418 scopus 로고    scopus 로고
    • Identification of a receptor-binding region within domain 4 of the protective antigen component of anthrax toxin
    • Varughese, M., Teixeira, A. V., Liu, S., and Leppla, S. H. (1999) Identification of a receptor-binding region within domain 4 of the protective antigen component of anthrax toxin Infect. Immun. 67, 1860-1865
    • (1999) Infect. Immun. , vol.67 , pp. 1860-1865
    • Varughese, M.1    Teixeira, A.V.2    Liu, S.3    Leppla, S.H.4
  • 7
    • 2542445481 scopus 로고    scopus 로고
    • Binding stoichiometry and kinetics of the interaction of a human anthrax toxin receptor, CMG2, with protective antigen
    • Wigelsworth, D. J., Krantz, B. A., Christensen, K. A., Lacy, D. B., Juris, S. J., and Collier, R. J. (2004) Binding stoichiometry and kinetics of the interaction of a human anthrax toxin receptor, CMG2, with protective antigen J. Biol. Chem. 279, 23349-23356
    • (2004) J. Biol. Chem. , vol.279 , pp. 23349-23356
    • Wigelsworth, D.J.1    Krantz, B.A.2    Christensen, K.A.3    Lacy, D.B.4    Juris, S.J.5    Collier, R.J.6
  • 8
    • 84866624076 scopus 로고    scopus 로고
    • PH effects on binding between the anthrax protective antigen and the host cellular receptor CMG2
    • Rajapaksha, M., Lovell, S., Janowiak, B. E., Andra, K. K., Battaile, K. P., and Bann, J. G. (2012) pH effects on binding between the anthrax protective antigen and the host cellular receptor CMG2 Protein Sci. 21, 1467-1480
    • (2012) Protein Sci. , vol.21 , pp. 1467-1480
    • Rajapaksha, M.1    Lovell, S.2    Janowiak, B.E.3    Andra, K.K.4    Battaile, K.P.5    Bann, J.G.6
  • 9
    • 36048985281 scopus 로고    scopus 로고
    • Anthrax toxin receptor 2 determinants that dictate the pH threshold of toxin pore formation
    • Scobie, H. M., Marlett, J. M., Rainey, G. J., Lacy, D. B., Collier, R. J., and Young, J. A. (2007) Anthrax toxin receptor 2 determinants that dictate the pH threshold of toxin pore formation PLoS One 2, e329
    • (2007) PLoS One , vol.2 , pp. 329
    • Scobie, H.M.1    Marlett, J.M.2    Rainey, G.J.3    Lacy, D.B.4    Collier, R.J.5    Young, J.A.6
  • 11
    • 84893695929 scopus 로고    scopus 로고
    • 19F nuclear magnetic resonance and crystallographic studies of 5-fluorotryptophan-labeled anthrax protective antigen and effects of the receptor on stability
    • 19F nuclear magnetic resonance and crystallographic studies of 5-fluorotryptophan-labeled anthrax protective antigen and effects of the receptor on stability Biochemistry 53, 690-701
    • (2014) Biochemistry , vol.53 , pp. 690-701
    • Chadegani, F.1    Lovell, S.2    Mullangi, V.3    Miyagi, M.4    Battaile, K.P.5    Bann, J.G.6
  • 12
    • 51549109753 scopus 로고    scopus 로고
    • avalues of individual histidine residues in proteins using mass spectrometry
    • avalues of individual histidine residues in proteins using mass spectrometry Anal. Chem. 80, 6481-6487
    • (2008) Anal. Chem. , vol.80 , pp. 6481-6487
    • Miyagi, M.1    Nakazawa, T.2
  • 13
    • 84856747211 scopus 로고    scopus 로고
    • Slow histidine H/D exchange protocol for thermodynamic analysis of protein folding and stability using mass spectrometry
    • Tran, D. T., Banerjee, S., Alayash, A. I., Crumbliss, A. L., and Fitzgerald, M. C. (2012) Slow histidine H/D exchange protocol for thermodynamic analysis of protein folding and stability using mass spectrometry Anal. Chem. 84, 1653-1660
    • (2012) Anal. Chem. , vol.84 , pp. 1653-1660
    • Tran, D.T.1    Banerjee, S.2    Alayash, A.I.3    Crumbliss, A.L.4    Fitzgerald, M.C.5
  • 17
    • 79951890355 scopus 로고    scopus 로고
    • Histidine hydrogen-deuterium exchange mass spectrometry for probing the microenvironment of histidine residues in dihydrofolate reductase
    • Miyagi, M., Wan, Q., Ahmad, M. F., Gokulrangan, G., Tomechko, S. E., Bennett, B., and Dealwis, C. (2011) Histidine hydrogen-deuterium exchange mass spectrometry for probing the microenvironment of histidine residues in dihydrofolate reductase PLoS One 6, e17055
    • (2011) PLoS One , vol.6 , pp. 17055
    • Miyagi, M.1    Wan, Q.2    Ahmad, M.F.3    Gokulrangan, G.4    Tomechko, S.E.5    Bennett, B.6    Dealwis, C.7
  • 18
    • 34247239927 scopus 로고    scopus 로고
    • Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. Coli: Modulation of conformational ensembles without altering structure or stability
    • Young, T. A., Skordalakes, E., and Marqusee, S. (2007) Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: Modulation of conformational ensembles without altering structure or stability J. Mol. Biol. 368, 1438-1447
    • (2007) J. Mol. Biol. , vol.368 , pp. 1438-1447
    • Young, T.A.1    Skordalakes, E.2    Marqusee, S.3
  • 19
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R. and Braun, W. (1998) Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules J. Comput. Chem. 19, 319-333
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 20
    • 0033578445 scopus 로고    scopus 로고
    • Atomic mutations at the single tryptophan residue of human recombinant annexin V: Effects on structure, stability, and activity
    • Minks, C., Huber, R., Moroder, L., and Budisa, N. (1999) Atomic mutations at the single tryptophan residue of human recombinant annexin V: Effects on structure, stability, and activity Biochemistry 38, 10649-10659
    • (1999) Biochemistry , vol.38 , pp. 10649-10659
    • Minks, C.1    Huber, R.2    Moroder, L.3    Budisa, N.4
  • 21
    • 0014410525 scopus 로고
    • Comparison of the specificities of various neutral proteinases from microorganisms
    • Morihara, K., Tsuzuki, H., and Oka, T. (1968) Comparison of the specificities of various neutral proteinases from microorganisms Arch. Biochem. Biophys. 123, 572-588
    • (1968) Arch. Biochem. Biophys. , vol.123 , pp. 572-588
    • Morihara, K.1    Tsuzuki, H.2    Oka, T.3
  • 23
    • 0000339601 scopus 로고
    • The kinetics of deuteration of imidazole
    • Vaughan, J. D., Mughrabi, Z. E., and Wu, C. (1970) The kinetics of deuteration of imidazole J. Org. Chem. 35, 1141-1145
    • (1970) J. Org. Chem. , vol.35 , pp. 1141-1145
    • Vaughan, J.D.1    Mughrabi, Z.E.2    Wu, C.3
  • 24
    • 0015915315 scopus 로고
    • Hydrogen-deuterium exchange kinetics of the C-2 protons of imidazole and histidine compounds
    • Bradbury, J. H., Chapman, B. E., and Pellegrino, F. A. (1973) Hydrogen-deuterium exchange kinetics of the C-2 protons of imidazole and histidine compounds J. Am. Chem. Soc. 95, 6139-6140
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 6139-6140
    • Bradbury, J.H.1    Chapman, B.E.2    Pellegrino, F.A.3
  • 25
    • 84855254449 scopus 로고    scopus 로고
    • Domain flexibility modulates the heterogeneous assembly mechanism of anthrax toxin protective antigen
    • Feld, G. K., Kintzer, A. F., Tang, I. I., Thoren, K. L., and Krantz, B. A. (2012) Domain flexibility modulates the heterogeneous assembly mechanism of anthrax toxin protective antigen J. Mol. Biol. 415, 159-174
    • (2012) J. Mol. Biol. , vol.415 , pp. 159-174
    • Feld, G.K.1    Kintzer, A.F.2    Tang, I.I.3    Thoren, K.L.4    Krantz, B.A.5
  • 26
    • 78650563014 scopus 로고    scopus 로고
    • Progress and novel strategies in vaccine development and treatment of anthrax
    • Chitlaru, T., Altboum, Z., Reuveny, S., and Shafferman, A. (2011) Progress and novel strategies in vaccine development and treatment of anthrax Immunol. Rev. 239, 221-236
    • (2011) Immunol. Rev. , vol.239 , pp. 221-236
    • Chitlaru, T.1    Altboum, Z.2    Reuveny, S.3    Shafferman, A.4
  • 27
    • 2142647811 scopus 로고    scopus 로고
    • Conformational dynamics of the GdmHCl-induced molten globule state of creatine kinase monitored by hydrogen exchange and mass spectrometry
    • Mazon, H., Marcillat, O., Forest, E., Smith, D. L., and Vial, C. (2004) Conformational dynamics of the GdmHCl-induced molten globule state of creatine kinase monitored by hydrogen exchange and mass spectrometry Biochemistry 43, 5045-5054
    • (2004) Biochemistry , vol.43 , pp. 5045-5054
    • Mazon, H.1    Marcillat, O.2    Forest, E.3    Smith, D.L.4    Vial, C.5
  • 28
    • 20444379285 scopus 로고    scopus 로고
    • Denaturant sensitive regions in creatine kinase identified by hydrogen/deuterium exchange
    • Mazon, H., Marcillat, O., Forest, E., and Vial, C. (2005) Denaturant sensitive regions in creatine kinase identified by hydrogen/deuterium exchange Rapid Commun. Mass Spectrom. 19, 1461-1468
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 1461-1468
    • Mazon, H.1    Marcillat, O.2    Forest, E.3    Vial, C.4
  • 29
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann, L., Pan, J., and Liu, Y. H. (2011) Hydrogen exchange mass spectrometry for studying protein structure and dynamics Chem. Soc. Rev. 40, 1224-1234
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 30
    • 0242286689 scopus 로고    scopus 로고
    • The kinetics of side chain stabilization during protein folding
    • Frieden, C. (2003) The kinetics of side chain stabilization during protein folding Biochemistry 42, 12439-12446
    • (2003) Biochemistry , vol.42 , pp. 12439-12446
    • Frieden, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.