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Volumn 350, Issue 4, 2005, Pages 735-743

Crystal structure of a CRISP family Ca2+-channel blocker derived from snake venom

Author keywords

Ca2+ channel blocker; CRISP; Crystal structure; Snake venom; Trifling

Indexed keywords

CADMIUM; CALCIUM CHANNEL; CALCIUM CHANNEL BLOCKING AGENT; CYSTEINE; CYSTEINE RICH SECRETORY PROTEIN; GLUTAMIC ACID; HISTIDINE; ION CHANNEL; POTASSIUM CHANNEL BLOCKING AGENT; POTASSIUM ION; SECRETORY PROTEIN; SNAKE VENOM; TRIFLIN; UNCLASSIFIED DRUG;

EID: 20544476609     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.020     Document Type: Article
Times cited : (91)

References (37)
  • 1
    • 0019547287 scopus 로고
    • Isolation, culture, and immunocytochemical characterization of epididymal epithelial cells from pubertal and adult rats
    • A.L. Kierszenbaum, O. Lea, P. Petrusz, F.S. French, and L.L. Tres Isolation, culture, and immunocytochemical characterization of epididymal epithelial cells from pubertal and adult rats Proc. Natl Acad. Sci. USA 78 1981 1675 1679
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 1675-1679
    • Kierszenbaum, A.L.1    Lea, O.2    Petrusz, P.3    French, F.S.4    Tres, L.L.5
  • 2
    • 0023759494 scopus 로고
    • Molecular cloning of complementary deoxyribonucleic acid for an androgen-regulated epididymal protein: Sequence homology with metalloproteins
    • N.J. Charest, D.R. Joseph, E.M. Wilson, and F.S. French Molecular cloning of complementary deoxyribonucleic acid for an androgen-regulated epididymal protein: sequence homology with metalloproteins Mol. Endocrinol. 2 1988 999 1004
    • (1988) Mol. Endocrinol. , vol.2 , pp. 999-1004
    • Charest, N.J.1    Joseph, D.R.2    Wilson, E.M.3    French, F.S.4
  • 3
    • 0036785275 scopus 로고    scopus 로고
    • Expression and structure-function analysis of de, a sperm cysteine-rich secretory protein that mediates gamete fusion
    • D.A. Ellerman, V.G. Da Ros, D.J. Cohen, D. Busso, M.M. Morgenfeld, and P.S. Cuasnicu Expression and structure-function analysis of de, a sperm cysteine-rich secretory protein that mediates gamete fusion Biol. Reprod. 67 2002 1225 1231
    • (2002) Biol. Reprod. , vol.67 , pp. 1225-1231
    • Ellerman, D.A.1    Da Ros, V.G.2    Cohen, D.J.3    Busso, D.4    Morgenfeld, M.M.5    Cuasnicu, P.S.6
  • 4
    • 0024742682 scopus 로고
    • Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene. a testis-specific gene Tpx-1 maps between Pgk-2 and Mep-1 on mouse chromosome 17
    • M. Kasahara, J. Gutknecht, K. Brew, N. Spurr, P.N. Goodfellow, H.C. Passmore, and J. Klein Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene. A testis-specific gene Tpx-1 maps between Pgk-2 and Mep-1 on mouse chromosome 17 Genomics 5 1989 527 534
    • (1989) Genomics , vol.5 , pp. 527-534
    • Kasahara, M.1    Gutknecht, J.2    Brew, K.3    Spurr, N.4    Goodfellow, P.N.5    Passmore, H.C.6    Klein, J.7
  • 5
    • 0030020880 scopus 로고    scopus 로고
    • SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis-specific gene product and a rodent sperm-coating glycoprotein
    • L. Kjeldsen, J.B. Cowland, A.H. Johnsen, and N. Borregaard SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis-specific gene product and a rodent sperm-coating glycoprotein FEBS Letters 380 1996 246 250
    • (1996) FEBS Letters , vol.380 , pp. 246-250
    • Kjeldsen, L.1    Cowland, J.B.2    Johnsen, A.H.3    Borregaard, N.4
  • 6
    • 0025259449 scopus 로고
    • Isolation and characterization of helothermine, a novel toxin from Heloderma horridum horridum (Mexican beaded lizard) venom
    • J. Mochca-Morales, B.M. Martin, and L.D. Possani Isolation and characterization of helothermine, a novel toxin from Heloderma horridum horridum (Mexican beaded lizard) venom Toxicon 28 1990 299 309
    • (1990) Toxicon , vol.28 , pp. 299-309
    • Mochca-Morales, J.1    Martin, B.M.2    Possani, L.D.3
  • 9
    • 0030001460 scopus 로고    scopus 로고
    • Helothermine, a lizard venom toxin, inhibits calcium current in cerebellar granules
    • M. Nobile, F. Noceti, G. Prestipino, and L.D. Possani Helothermine, a lizard venom toxin, inhibits calcium current in cerebellar granules Expt. Brain Res. 110 1996 15 20
    • (1996) Expt. Brain Res. , vol.110 , pp. 15-20
    • Nobile, M.1    Noceti, F.2    Prestipino, G.3    Possani, L.D.4
  • 11
    • 0037418579 scopus 로고    scopus 로고
    • Identification of a DAF-16 transcriptional target gene, scl-1, that regulates longevity and stress resistance in Caenorhabditis elegans
    • S. Ookuma, M. Fukuda, and E. Nishida Identification of a DAF-16 transcriptional target gene, scl-1, that regulates longevity and stress resistance in Caenorhabditis elegans Curr. Biol. 13 2003 427 431
    • (2003) Curr. Biol. , vol.13 , pp. 427-431
    • Ookuma, S.1    Fukuda, M.2    Nishida, E.3
  • 13
    • 0035576365 scopus 로고    scopus 로고
    • Major venom allergen of yellow jackets. Ves v 5: Structural characterization of a pathogenesis-related protein superfamily
    • A. Henriksen, T.P. King, O. Mirza, R.I. Monsalve, K. Meno, and H. Ipsen Major venom allergen of yellow jackets. Ves v 5: structural characterization of a pathogenesis-related protein superfamily Proteins: Struct. Funct. Genet. 45 2001 438 448
    • (2001) Proteins: Struct. Funct. Genet. , vol.45 , pp. 438-448
    • Henriksen, A.1    King, T.P.2    Mirza, O.3    Monsalve, R.I.4    Meno, K.5    Ipsen, H.6
  • 14
    • 4043092774 scopus 로고    scopus 로고
    • Structure and function of snake venom cysteine-rich secretory proteins
    • Y. Yamazaki, and T. Morita Structure and function of snake venom cysteine-rich secretory proteins Toxicon 44 2004 227 231
    • (2004) Toxicon , vol.44 , pp. 227-231
    • Yamazaki, Y.1    Morita, T.2
  • 15
    • 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
    • Y. Yamazaki, F. Hyodo, and T. Morita 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 2003 133 141
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 133-141
    • Yamazaki, Y.1    Hyodo, F.2    Morita, T.3
  • 16
    • 0036272410 scopus 로고    scopus 로고
    • Cloning and characterization of novel snake venom proteins that block smooth muscle contraction
    • Y. Yamazaki, H. Koike, Y. Sugiyama, K. Motoyoshi, T. Wada, and S. Hishinuma Cloning and characterization of novel snake venom proteins that block smooth muscle contraction Eur. J. Biochem. 269 2002 2708 2715
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2708-2715
    • Yamazaki, Y.1    Koike, H.2    Sugiyama, Y.3    Motoyoshi, K.4    Wada, T.5    Hishinuma, S.6
  • 17
    • 0033582176 scopus 로고    scopus 로고
    • Pseudechetoxin: A peptide blocker of cyclic nucleotide-gated ion channels
    • R.L. Brown, T.L. Haley, K.A. West, and J.W. Crabb Pseudechetoxin: a peptide blocker of cyclic nucleotide-gated ion channels Proc. Natl Acad. Sci. USA 96 1999 754 759
    • (1999) Proc. Natl Acad. Sci. USA , 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
    • Y. Yamazaki, R.L. Brown, and T. Morita Purification and cloning of toxins from elapid venoms that target cyclic nucleotide-gated ion channels Biochemistry 41 2002 11331 11337
    • (2002) Biochemistry , vol.41 , pp. 11331-11337
    • Yamazaki, Y.1    Brown, R.L.2    Morita, T.3
  • 19
    • 0344304501 scopus 로고    scopus 로고
    • Pseudechetoxin binds to the pore turret of cyclic nucleotide-gated ion channels
    • R.L. Brown, L.L. Lynch, T.L. Haley, and R. Arsanjani Pseudechetoxin binds to the pore turret of cyclic nucleotide-gated ion channels J. Gen. Physiol. 122 2003 749 760
    • (2003) J. Gen. Physiol. , vol.122 , pp. 749-760
    • Brown, R.L.1    Lynch, L.L.2    Haley, T.L.3    Arsanjani, R.4
  • 20
    • 0034737306 scopus 로고    scopus 로고
    • Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: Common surface features of gating modifier toxins
    • H. Takahashi, J.I. Kim, H.J. Min, K. Sato, K.J. Swartz, and I. Shimada Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins J. Mol. Biol. 297 2000 771 780
    • (2000) J. Mol. Biol. , vol.297 , pp. 771-780
    • Takahashi, H.1    Kim, J.I.2    Min, H.J.3    Sato, K.4    Swartz, K.J.5    Shimada, I.6
  • 21
    • 0942279703 scopus 로고    scopus 로고
    • Solution structure and functional characterization of SGTx1, a modifier of Kv2.1 channel gating
    • C.W. Lee, S. Kim, S.H. Roh, H. Endoh, Y. Kodera, and T. Maeda Solution structure and functional characterization of SGTx1, a modifier of Kv2.1 channel gating Biochemistry 43 2004 890 897
    • (2004) Biochemistry , vol.43 , pp. 890-897
    • Lee, C.W.1    Kim, S.2    Roh, S.H.3    Endoh, H.4    Kodera, Y.5    Maeda, T.6
  • 22
    • 3142580385 scopus 로고    scopus 로고
    • A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom
    • S.Y. Lee, and R. MacKinnon A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom Nature 430 2004 232 235
    • (2004) Nature , vol.430 , pp. 232-235
    • Lee, S.Y.1    MacKinnon, R.2
  • 23
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • M. Gerstein, A.M. Lesk, and C. Chothia Structural mechanisms for domain movements in proteins Biochemistry 33 1994 6739 6749
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 24
    • 0032478175 scopus 로고    scopus 로고
    • Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system
    • T. Szyperski, C. Fernandez, C. Mumenthaler, and K. Wuthrich Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system Proc. Natl Acad. Sci. USA 95 1998 2262 2266
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2262-2266
    • Szyperski, T.1    Fernandez, C.2    Mumenthaler, C.3    Wuthrich, K.4
  • 25
    • 0041731780 scopus 로고    scopus 로고
    • Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily
    • T.J. Milne, G. Abbenante, J.D. Tyndall, J. Halliday, and R.J. Lewis Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily J. Biol. Chem. 278 2003 31105 31110
    • (2003) J. Biol. Chem. , vol.278 , pp. 31105-31110
    • Milne, T.J.1    Abbenante, G.2    Tyndall, J.D.3    Halliday, J.4    Lewis, R.J.5
  • 26
    • 0028887525 scopus 로고
    • Phenylephrine contracts rat tail artery by one electromechanical and three pharmacomechanical mechanisms
    • X.L. Chen, and C.M. Rembold Phenylephrine contracts rat tail artery by one electromechanical and three pharmacomechanical mechanisms Am. J. Physiol. 268 1995 H74 H81
    • (1995) Am. J. Physiol. , vol.268
    • Chen, X.L.1    Rembold, C.M.2
  • 27
  • 28
    • 0036606183 scopus 로고    scopus 로고
    • Membrane depolarization-induced contraction of rat caudal arterial smooth muscle involves Rho-associated kinase
    • M. Mita, H. Yanagihara, S. Hishinuma, M. Saito, and M.P. Walsh Membrane depolarization-induced contraction of rat caudal arterial smooth muscle involves Rho-associated kinase Biochem. J. 364 2002 431 440
    • (2002) Biochem. J. , vol.364 , pp. 431-440
    • Mita, M.1    Yanagihara, H.2    Hishinuma, S.3    Saito, M.4    Walsh, M.P.5
  • 29
    • 0029984862 scopus 로고    scopus 로고
    • A novel hydrophobic omega-conotoxin blocks molluscan dihydropyridine- sensitive calcium channels
    • M. Fainzilber, J.C. Lodder, R.C. van der Schors, K.W. Li, Z. Yu, and A.L. Burlingame A novel hydrophobic omega-conotoxin blocks molluscan dihydropyridine-sensitive calcium channels Biochemistry 35 1996 8748 8752
    • (1996) Biochemistry , vol.35 , pp. 8748-8752
    • Fainzilber, M.1    Lodder, J.C.2    Van Der Schors, R.C.3    Li, K.W.4    Yu, Z.5    Burlingame, A.L.6
  • 30
    • 0030973424 scopus 로고    scopus 로고
    • Structure-function relationships of omega-conotoxin GVIA. Synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues
    • M.J. Lew, J.P. Flinn, P.K. Pallaghy, R. Murphy, S.L. Whorlow, and C.E. Wright Structure-function relationships of omega-conotoxin GVIA. Synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues J. Biol. Chem. 272 1997 12014 12023
    • (1997) J. Biol. Chem. , vol.272 , pp. 12014-12023
    • Lew, M.J.1    Flinn, J.P.2    Pallaghy, P.K.3    Murphy, R.4    Whorlow, S.L.5    Wright, C.E.6
  • 32
    • 0037044313 scopus 로고    scopus 로고
    • Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel, Kv1.3
    • M.D. Lanigan, K. Kalman, Y. Lefievre, M.W. Pennington, K.G. Chandy, and R.S. Norton Mutating a critical lysine in ShK toxin alters its binding configuration in the pore-vestibule region of the voltage-gated potassium channel, Kv1.3 Biochemistry 41 2002 11963 11971
    • (2002) Biochemistry , vol.41 , pp. 11963-11971
    • Lanigan, M.D.1    Kalman, K.2    Lefievre, Y.3    Pennington, M.W.4    Chandy, K.G.5    Norton, R.S.6
  • 33
    • 0033618255 scopus 로고    scopus 로고
    • Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin
    • H. Rauer, M. Pennington, M. Cahalan, and K.G. Chandy Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin J. Biol. Chem. 274 1999 21885 21892
    • (1999) J. Biol. Chem. , vol.274 , pp. 21885-21892
    • Rauer, H.1    Pennington, M.2    Cahalan, M.3    Chandy, K.G.4
  • 34
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 35
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N
    • Collaborative Computational Project, N The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 36
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • J.C.W. Carter R.M. Sweet Academic Press New York
    • E. de La Fortelle, and G. Bricogne Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods J.C.W. Carter R.M. Sweet Methods Enzymology 1997 Academic Press New York 472 494
    • (1997) Methods Enzymology , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2


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