메뉴 건너뛰기




Volumn 44, Issue 30, 2005, Pages 10145-10152

Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CALCIUM COMPOUNDS; CONCENTRATION (PROCESS); CRYSTAL STRUCTURE; POTASSIUM;

EID: 23044468262     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050614m     Document Type: Article
Times cited : (95)

References (39)
  • 1
    • 0029108913 scopus 로고
    • Physiological roles and properties of potassium channels in arterial smooth muscle
    • Nelson, M. T., and Quayle, J. M. (1995) Physiological roles and properties of potassium channels in arterial smooth muscle. Am. J. Physiol. 268, 799-822.
    • (1995) Am. J. Physiol. , vol.268 , pp. 799-822
    • Nelson, M.T.1    Quayle, J.M.2
  • 2
    • 0036525417 scopus 로고    scopus 로고
    • Modulation of calcium-activated potassium channels
    • Weiger, T. M., Hermann, A. L., and Evitan, I. B. (2002) Modulation of calcium-activated potassium channels, J. Comp. Physiol., A 188, 79-87.
    • (2002) J. Comp. Physiol., A , vol.188 , pp. 79-87
    • Weiger, T.M.1    Hermann, A.L.2    Evitan, I.B.3
  • 3
    • 0033977162 scopus 로고    scopus 로고
    • Ion channels and vascular tone
    • Jackson, W. F. (2000) Ion channels and vascular tone, Hypertension 35, 173-178.
    • (2000) Hypertension , vol.35 , pp. 173-178
    • Jackson, W.F.1
  • 4
    • 0029931330 scopus 로고    scopus 로고
    • High-conductance calcium-activated potassium channels; structure, pharmacology, and function
    • Gregory, J. K., Hans-Gunther, K., Reid, J. L., Owen, B. M., and Maria, L. G. (1996) High-conductance calcium-activated potassium channels; structure, pharmacology, and function, J. Bioenerg. Biomembr. 28, 255-267.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 255-267
    • Gregory, J.K.1    Hans-Gunther, K.2    Reid, J.L.3    Owen, B.M.4    Maria, L.G.5
  • 5
    • 0032055663 scopus 로고    scopus 로고
    • 2+] in cerebral arteries of rat by membrane potential and intravascular pressure
    • 2+] in cerebral arteries of rat by membrane potential and intravascular pressure, J. Physiol. 508, 199-209.
    • (1998) J. Physiol. , vol.508 , pp. 199-209
    • Knot, H.J.1    Nelson, M.T.2
  • 8
    • 0033635776 scopus 로고    scopus 로고
    • Potassium channels: Molecular defects, diseases, and therapeutic opportunities
    • Shieh, C.-C., Coghlan, M., Sullivan, J. P., and Gopalakrishnan, M. (2000) Potassium channels: Molecular defects, diseases, and therapeutic opportunities, Pharmacol. Rev. 52, 557-593.
    • (2000) Pharmacol. Rev. , vol.52 , pp. 557-593
    • Shieh, C.-C.1    Coghlan, M.2    Sullivan, J.P.3    Gopalakrishnan, M.4
  • 9
    • 0027161159 scopus 로고
    • mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels
    • Butler, A., Tsunoda, S., McCobb, D. P., Wei, A., and Salkoff, L. (1993) mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels, Science 261, 221-224.
    • (1993) Science , vol.261 , pp. 221-224
    • Butler, A.1    Tsunoda, S.2    McCobb, D.P.3    Wei, A.4    Salkoff, L.5
  • 12
    • 0006117915 scopus 로고
    • Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels
    • Gimenez, G., Navia, M. A., Reuben, J. P., Katz, G. M., Kaczorowski, G. J., and Garcia, M. L. (1988) Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels, Proc. Natl. Acad. Sci. U.S.A. 85, 3329-3333.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3329-3333
    • Gimenez, G.1    Navia, M.A.2    Reuben, J.P.3    Katz, G.M.4    Kaczorowski, G.J.5    Garcia, M.L.6
  • 13
    • 0028117321 scopus 로고
    • + channel structure from a complete functional map of the molecular surface of charybdotoxin
    • + channel structure from a complete functional map of the molecular surface of charybdotoxin, Biochemistry 33, 443-450.
    • (1994) Biochemistry , vol.33 , pp. 443-450
    • Stampe, P.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 16
    • 16644394108 scopus 로고    scopus 로고
    • Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegerivenoms
    • Wang, J., Guo, M., Tu, X. Y., Zheng, D. R, Teng, M. K., Niu, L. W., Liu, Q., Huang, Q. Q., and Hao, Q. (2004) Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegerivenoms, Acta Crystallogr. D60, 1108-1111.
    • (2004) Acta Crystallogr. , vol.D60 , pp. 1108-1111
    • Wang, J.1    Guo, M.2    Tu, X.Y.3    Zheng, D.R.4    Teng, M.K.5    Niu, L.W.6    Liu, Q.7    Huang, Q.Q.8    Hao, Q.9
  • 17
    • 0033582176 scopus 로고    scopus 로고
    • Pseudechetoxin: A peptide blocker of cyclic nucleotide-gated ion channels
    • Brown, R. L., Haley, T. L., West, K. A., and Crabb, J. W. (1999) Pseudechetoxin: A peptide blocker of cyclic nucleotide-gated ion channels, Proc. Natl. Acad. Sci. U.S.A. 96, 754-759.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 754-759
    • Brown, R.L.1    Haley, T.L.2    West, K.A.3    Crabb, J.W.4
  • 18
    • 0037167616 scopus 로고    scopus 로고
    • Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels
    • Yamazaki, Y., Brown, R. L., and Morita, T. (2002) Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels, Biochemistry 41, 11331-11337.
    • (2002) Biochemistry , vol.41 , pp. 11331-11337
    • Yamazaki, Y.1    Brown, R.L.2    Morita, T.3
  • 24
    • 0029878263 scopus 로고    scopus 로고
    • Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone
    • Tudor, J. E., Pallaghy, P. K., Pennington, M. W., and Norton, R. S. (1996) Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone, Nat. Struct. Biol. 3. 317-320.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 317-320
    • Tudor, J.E.1    Pallaghy, P.K.2    Pennington, M.W.3    Norton, R.S.4
  • 25
    • 2942600224 scopus 로고    scopus 로고
    • An increase in opening of BKCa channels in smooth muscle cells in streptozotocin induced diabetic mice
    • Ye, C. L., Shen, B., Ren, X. D., Luo, R. J., Ding, S. Y., Yan, F. M., and Jiang, J. H. (2004) An increase in opening of BKCa channels in smooth muscle cells in streptozotocin induced diabetic mice, Acta Pharmacol. Sin. 25, 744-750.
    • (2004) Acta Pharmacol. Sin. , vol.25 , pp. 744-750
    • Ye, C.L.1    Shen, B.2    Ren, X.D.3    Luo, R.J.4    Ding, S.Y.5    Yan, F.M.6    Jiang, J.H.7
  • 26
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navazza, J. (1994) AMoRe: An automated package for molecular replacement, Acta Crystallogr. B50, 157-163.
    • (1994) Acta Crystallogr. , vol.B50 , pp. 157-163
    • Navazza, J.1
  • 27
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P., Grosse-Kunstleve, R. W., et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination, Acta Crystallogr. D54, 905-921.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3    Delano, W.L.4    Gros, P.5    Grosse-Kunstleve, R.W.6
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kleldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kleldgaard, M.4
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structure
    • Laskowski, R. A., MacArthur, M. V., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structure, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.V.2    Moss, D.S.3    Thornton, J.M.4
  • 30
    • 0141608994 scopus 로고    scopus 로고
    • + channels of the coronary artery during left ventricular hypertrophy
    • + channels of the coronary artery during left ventricular hypertrophy, Circ. Res. 93, 541-547.
    • (2003) Circ. Res. , vol.93 , pp. 541-547
    • Kim, N.1    Chung, J.2    Kim, E.3    Han, J.4
  • 31
    • 0033082090 scopus 로고    scopus 로고
    • + channels and non-selective cation channels to membrane potential of pulmonary arterial smooth muscle cells of the rabbit
    • + channels and non-selective cation channels to membrane potential of pulmonary arterial smooth muscle cells of the rabbit, J. Physiol. 514, 747-758.
    • (1999) J. Physiol. , vol.514 , pp. 747-758
    • Bae, Y.M.1    Park, M.K.2    Lee, S.H.3    Ho, W.K.4    Earm, Y.E.5
  • 32
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change, new results on citrate synthase and T4 lysozyme
    • Hayward, S., and Berendsen, H. J. C. (1998) Systematic analysis of domain motions in proteins from conformational change, new results on citrate synthase and T4 lysozyme, Proteins 30, 144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.C.2
  • 33
    • 0028887525 scopus 로고
    • Phenylephrine contracts rat tail artery by one electromechanical and three pharmacomechanical mechanisms
    • Chen, X. L., and Rembold, C. M. (1995) Phenylephrine contracts rat tail artery by one electromechanical and three pharmacomechanical mechanisms, Am. J. Physiol. 268, H74-H81.
    • (1995) Am. J. Physiol. , vol.268
    • Chen, X.L.1    Rembold, C.M.2
  • 34
    • 0026575435 scopus 로고
    • Regulation of arterial tone by activation of calcium-dependent potassium channels
    • Brayden, J. E., and Nelson, M. T. (1992) Regulation of arterial tone by activation of calcium-dependent potassium channels, Science 256, 532-535.
    • (1992) Science , vol.256 , pp. 532-535
    • Brayden, J.E.1    Nelson, M.T.2
  • 35
    • 4043092774 scopus 로고    scopus 로고
    • Structure and function of snake venom cysteine-rich secretory proteins
    • Yamazaki, Y., and Monta, T. (2004) Structure and function of snake venom cysteine-rich secretory proteins, Toxicon 44, 227-231.
    • (2004) Toxicon , vol.44 , pp. 227-231
    • Yamazaki, Y.1    Monta, T.2
  • 36
    • 0031922657 scopus 로고    scopus 로고
    • Conformation dynamics and enzyme activity
    • Yon, J. M., Perahia, D., and Ghelis, C. (1998) Conformation dynamics and enzyme activity, Biochimie 80, 33-42.
    • (1998) Biochimie , vol.80 , pp. 33-42
    • Yon, J.M.1    Perahia, D.2    Ghelis, C.3
  • 37
    • 0032530836 scopus 로고    scopus 로고
    • A database of macromolecular motions
    • Gerstein, M., and Krebs, W. (1998) A database of macromolecular motions, Nucleic Acids Res. 26, 4280-4290.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4280-4290
    • Gerstein, M.1    Krebs, W.2
  • 38
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A. M., and Chothia, C. (1994) Structural mechanisms for domain movements in proteins, Biochemistry 33, 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 39
    • 0037376935 scopus 로고    scopus 로고
    • Wide distribution of cysteine-rich secretory proteins in snake venoms: Isolation and cloning of novel snake venom cysteine-rich secretory proteins
    • Yamazaki, Y., Hyodo, F., and Morita, T. (2003) Wide distribution of cysteine-rich secretory proteins in snake venoms: Isolation and cloning of novel snake venom cysteine-rich secretory proteins, Arch. Biochem. Biophys. 412, 133-141.
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 133-141
    • Yamazaki, Y.1    Hyodo, F.2    Morita, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.