메뉴 건너뛰기




Volumn 57, Issue 4, 2004, Pages 839-849

Solution structure of γ-bungarotoxin: The functional significance of amino acid residues flanking the RGD motif in integrin binding

Author keywords

bungarotoxin; Disintegrin; Neurotoxin fold; NMR solution structure; RGD containing protein

Indexed keywords

ANTITHROMBOCYTIC AGENT; ARGINYLGLYCYLASPARTIC ACID; BUNGAROTOXIN; CYSTEINE; DISINTEGRIN; DISULFIDE; GAMMA BUNGAROTOXIN; INTEGRIN; NEUROTOXIN; RHODOSTOMIN; UNCLASSIFIED DRUG;

EID: 10344225605     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20269     Document Type: Article
Times cited : (35)

References (44)
  • 5
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol 1996;12:697-715.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 7
    • 0037077268 scopus 로고    scopus 로고
    • Savignygrin, a platelet aggregation inhibitor from the soft tick Ornifhodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold
    • Mans BJ, Louw AI, Neitz AW. Savignygrin, a platelet aggregation inhibitor from the soft tick Ornifhodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold. J Biol Chem 2002;277:21371-21378.
    • (2002) J Biol Chem , vol.277 , pp. 21371-21378
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.3
  • 9
    • 0037369082 scopus 로고    scopus 로고
    • Human herpesvirus 8 envelope glycoprotein B mediates cell adhesion via its RGD sequence
    • Wang FZ, Akula SM, Shanna-Walia N, Zeng L, Chandran B. Human herpesvirus 8 envelope glycoprotein B mediates cell adhesion via its RGD sequence. J Virol 2003;77:3131-3147.
    • (2003) J Virol , vol.77 , pp. 3131-3147
    • Wang, F.Z.1    Akula, S.M.2    Shanna-Walia, N.3    Zeng, L.4    Chandran, B.5
  • 10
    • 0026350087 scopus 로고
    • Solution structure of kistrin, a potent platelet aggregation inhibitor and GP Ub-IIIa antagonist
    • Adler M, Lazarus RA, Dennis MS, Wagner G. Solution structure of kistrin, a potent platelet aggregation inhibitor and GP Ub-IIIa antagonist. Science 1991;253:445-448.
    • (1991) Science , vol.253 , pp. 445-448
    • Adler, M.1    Lazarus, R.A.2    Dennis, M.S.3    Wagner, G.4
  • 11
    • 0025786742 scopus 로고
    • Three-dimensional structure of echistatin, the smallest active RGD protein
    • Saudek V, Atkinson RA, Pelton JT. Three-dimensional structure of echistatin, the smallest active RGD protein. Biochemistry 1991;30:7369-7372.
    • (1991) Biochemistry , vol.30 , pp. 7369-7372
    • Saudek, V.1    Atkinson, R.A.2    Pelton, J.T.3
  • 12
    • 0027165368 scopus 로고
    • The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP Ub-IIIa receptor
    • Senn H, Klaus W. The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP Ub-IIIa receptor. J Mol Biol 1993;232:907-925.
    • (1993) J Mol Biol , vol.232 , pp. 907-925
    • Senn, H.1    Klaus, W.2
  • 14
    • 0028017504 scopus 로고
    • Structure of the RGD protein decorsin: Conserved motif and distinct function in leech proteins that affect blood clotting
    • Krezel AM, Wagner G, Seymour-Ulmer J, Lazarus RA. Structure of the RGD protein decorsin: conserved motif and distinct function in leech proteins that affect blood clotting. Science 1994;264:1944-1947.
    • (1994) Science , vol.264 , pp. 1944-1947
    • Krezel, A.M.1    Wagner, G.2    Seymour-Ulmer, J.3    Lazarus, R.A.4
  • 15
    • 0028533579 scopus 로고
    • Three-dimensional structure of the RGD-containing neurotoxin homologue dendroaspin
    • Sutcliffe MJ, Jaseja M, Hyde EI, Lu X, Williams JA. Three-dimensional structure of the RGD-containing neurotoxin homologue dendroaspin. Nat Struct Biol 1994;1:802-807.
    • (1994) Nat Struct Biol , vol.1 , pp. 802-807
    • Sutcliffe, M.J.1    Jaseja, M.2    Hyde, E.I.3    Lu, X.4    Williams, J.A.5
  • 16
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy DJ, Aukhil I, Erickson HP. 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 1996;84:155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 17
    • 0028150753 scopus 로고
    • Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors
    • Niewiarowski S, McLane MA, Kloczewiak M, Stewart GJ. Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors. Semin Hematol 1994;31:289-300.
    • (1994) Semin Hematol , vol.31 , pp. 289-300
    • Niewiarowski, S.1    McLane, M.A.2    Kloczewiak, M.3    Stewart, G.J.4
  • 18
    • 0032971155 scopus 로고    scopus 로고
    • Primary structure of gamma-bungarotoxin, a new postsynaptic neurotoxin from venom of Bungarus multicinctus
    • Aird SD, Womble GC, Yates JR 3rd, Griffin PR. Primary structure of gamma-bungarotoxin, a new postsynaptic neurotoxin from venom of Bungarus multicinctus. Toxicon 1999;37:609-625.
    • (1999) Toxicon , vol.37 , pp. 609-625
    • Aird, S.D.1    Womble, G.C.2    Yates III, J.R.3    Griffin, P.R.4
  • 19
    • 52649173771 scopus 로고    scopus 로고
    • Characterization and gene organization of Taiwan banded krait (Bungarus multicinctus) gamma-bungarotoxin
    • Chang LS, Chung C, Wu BN, Yang CC. Characterization and gene organization of Taiwan banded krait (Bungarus multicinctus) gamma-bungarotoxin. J Protein Chem 2002;21:223-229.
    • (2002) J Protein Chem , vol.21 , pp. 223-229
    • Chang, L.S.1    Chung, C.2    Wu, B.N.3    Yang, C.C.4
  • 20
    • 0026099011 scopus 로고
    • Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex
    • Huang TF, Sheu RR, Teng CM, Chen SW, Liu CS. Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex. J Biochem 1991;109:328-334.
    • (1991) J Biochem , vol.109 , pp. 328-334
    • Huang, T.F.1    Sheu, R.R.2    Teng, C.M.3    Chen, S.W.4    Liu, C.S.5
  • 22
    • 0034061227 scopus 로고    scopus 로고
    • The role of fibronectin deposition in branching in tubulogenesis of MDCK cells
    • Jiang ST, Chuang WJ, Tang MJ. The role of fibronectin deposition in branching in tubulogenesis of MDCK cells. Kidney Int 2000;57:1860-1867.
    • (2000) Kidney Int , vol.57 , pp. 1860-1867
    • Jiang, S.T.1    Chuang, W.J.2    Tang, M.J.3
  • 23
    • 0029682812 scopus 로고    scopus 로고
    • Site-directed mutagenesis using overlap extension PCR
    • Aiyar A, Xiang Y, Leis J. Site-directed mutagenesis using overlap extension PCR. Methods Mol Biol 1996;57:177-191.
    • (1996) Methods Mol Biol , vol.57 , pp. 177-191
    • Aiyar, A.1    Xiang, Y.2    Leis, J.3
  • 24
    • 45249128810 scopus 로고
    • Measurement of vicinal couplings from cross peaks in COSY spectra
    • Kim Y, Prestegard JH. Measurement of vicinal couplings from cross peaks in COSY spectra. J Magn Reson 1989;84:9-13.
    • (1989) J Magn Reson , vol.84 , pp. 9-13
    • Kim, Y.1    Prestegard, J.H.2
  • 25
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner G, Braun W, Havel TF, Schaumann T, Go N, Wuthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J Mol Biol 1987;196:611-639.
    • (1987) J Mol Biol , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wuthrich, K.6
  • 27
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamic simulated annealing
    • Nilges M, Clore GM, Gronenborn AM. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamic simulated annealing. FEBS Lett 1988;229:129-136.
    • (1988) FEBS Lett , vol.229 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 28
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14:51-55.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 29
    • 0027236599 scopus 로고
    • Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. Application to flavoridin
    • Klaus W, Broger C, Gerber P, Senn H. Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. Application to flavoridin. J Mol Biol 1993;232:897-906.
    • (1993) J Mol Biol , vol.232 , pp. 897-906
    • Klaus, W.1    Broger, C.2    Gerber, P.3    Senn, H.4
  • 30
    • 0024291648 scopus 로고
    • Structural studies of alpha-bungarotoxin. 3. Corrections in the primary sequence and X-ray structure and characterization of an isotoxic alpha-bungarotoxin
    • Kosen PA, Finer-Moore J, McCarthy MP, Basus VJ. Structural studies of alpha-bungarotoxin. 3. Corrections in the primary sequence and X-ray structure and characterization of an isotoxic alpha-bungarotoxin. Biochemistry 1988;27:2775-2781.
    • (1988) Biochemistry , vol.27 , pp. 2775-2781
    • Kosen, P.A.1    Finer-Moore, J.2    McCarthy, M.P.3    Basus, V.J.4
  • 31
    • 0027944677 scopus 로고
    • Crystal structure of kappa-bungarotoxin at 2.3-Å resolution
    • Dewan JC, Grant GA, Sacchettini JC. Crystal structure of kappa-bungarotoxin at 2.3-Å resolution. Biochemistry 1994;44:13147-13154.
    • (1994) Biochemistry , vol.44 , pp. 13147-13154
    • Dewan, J.C.1    Grant, G.A.2    Sacchettini, J.C.3
  • 32
    • 0026451624 scopus 로고
    • Nuclear magnetic resonance solution structure of the alpha-neurotoxin from the black mamba (Dendroaspis polylepis polylepis)
    • Brown LR, Wuthrich K. Nuclear magnetic resonance solution structure of the alpha-neurotoxin from the black mamba (Dendroaspis polylepis polylepis). J Mol Biol 1992;227:1118-1135.
    • (1992) J Mol Biol , vol.227 , pp. 1118-1135
    • Brown, L.R.1    Wuthrich, K.2
  • 33
    • 0031010716 scopus 로고    scopus 로고
    • Three-dimensional solution structure of the complex of alpha-bungarotoxin with a library-derived peptide
    • Scherf T, Balass M, Fuchs S, Katchalski-Katzir E, Anglister J. Three-dimensional solution structure of the complex of alpha-bungarotoxin with a library-derived peptide. Proc Natl Acad Sci USA 1997;94:6059-6064.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6059-6064
    • Scherf, T.1    Balass, M.2    Fuchs, S.3    Katchalski-Katzir, E.4    Anglister, J.5
  • 35
    • 0025768399 scopus 로고
    • Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: Sequence-specific assignments, secondary structure, and dimer formation
    • Oswald RE, Sutcliffe MJ, Bamberger M, Loring, RH, Braswell E, Dobson CM. Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: sequence-specific assignments, secondary structure, and dimer formation. Biochemistry 1991;30:4901-4909.
    • (1991) Biochemistry , vol.30 , pp. 4901-4909
    • Oswald, R.E.1    Sutcliffe, M.J.2    Bamberger, M.3    Loring, R.H.4    Braswell, E.5    Dobson, C.M.6
  • 36
    • 0030570733 scopus 로고    scopus 로고
    • Importance of the structure of the RGB-containing loop in the disintegrins echistatin and eristostatin for recognition of alpha lib beta 3 and alpha v beta 3 integrins
    • McLane MA, Vijay-Kumar, S, Marcinkiewicz C, Calvete JJ, Niewiarowski S. Importance of the structure of the RGB-containing loop in the disintegrins echistatin and eristostatin for recognition of alpha lib beta 3 and alpha v beta 3 integrins. FEBS Lett 1996;391:139-143.
    • (1996) FEBS Lett , vol.391 , pp. 139-143
    • McLane, M.A.1    Vijay-Kumar, S.2    Marcinkiewicz, C.3    Calvete, J.J.4    Niewiarowski, S.5
  • 37
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptides of NMR defined conformation by alpha IIb beta 3, alpha V beta 3, and alpha 5 beta 1 integrins
    • Pfaff M, Tangemann K, Muller B, Gurrath M, Muller G, Kessler H, Timpl R, Engel J. Selective recognition of cyclic RGD peptides of NMR defined conformation by alpha IIb beta 3, alpha V beta 3, and alpha 5 beta 1 integrins. J Biol Chem 1994;269:20233-20238.
    • (1994) J Biol Chem , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Tangemann, K.2    Muller, B.3    Gurrath, M.4    Muller, G.5    Kessler, H.6    Timpl, R.7    Engel, J.8
  • 39
    • 0027465426 scopus 로고
    • Binding interactions of kistrin with platelet glycoprotein IIb-IIIa: Analysis by site-directed mutagenesis
    • Dennis MS, Carter P, Lazarus RA. Binding interactions of kistrin with platelet glycoprotein IIb-IIIa: analysis by site-directed mutagenesis. Proteins 1993;5:312-321.
    • (1993) Proteins , vol.5 , pp. 312-321
    • Dennis, M.S.1    Carter, P.2    Lazarus, R.A.3
  • 40
    • 0028972312 scopus 로고
    • The integrin alpha IIb beta 3 contains distinct and interacting binding sites for snakevenom RGD (Arg-Gly-Asp) proteins. Evidence that the receptor-binding characteristics of snake-venom RGD proteins are related to the amino acid environment flanking the sequence RGD
    • Rahman S, Lu X, Kakkar W, Authi KS. The integrin alpha IIb beta 3 contains distinct and interacting binding sites for snakevenom RGD (Arg-Gly-Asp) proteins. Evidence that the receptor-binding characteristics of snake-venom RGD proteins are related to the amino acid environment flanking the sequence RGD. Biochem J 1995;312:223-232.
    • (1995) Biochem J , vol.312 , pp. 223-232
    • Rahman, S.1    Lu, X.2    Kakkar, W.3    Authi, K.S.4
  • 41
    • 0032532104 scopus 로고    scopus 로고
    • Modulation of RGD sequence motifs regulates disintegrin recognition of alphallb beta3 and alpha5 beta1 integrin complexes. Replacement of elegantin alanine-50 with proline, N-terminal to the RGD sequence, diminishes recognition of the alpha5 beta1 complex with restoration induced by Mn2+ cation
    • Rahman S, Aitken A, Flynn G, Formstone C, Savidge GF. Modulation of RGD sequence motifs regulates disintegrin recognition of alphallb beta3 and alpha5 beta1 integrin complexes. Replacement of elegantin alanine-50 with proline, N-terminal to the RGD sequence, diminishes recognition of the alpha5 beta1 complex with restoration induced by Mn2+ cation. Biochem J 1998;335:247-257.
    • (1998) Biochem J , vol.335 , pp. 247-257
    • Rahman, S.1    Aitken, A.2    Flynn, G.3    Formstone, C.4    Savidge, G.F.5
  • 42
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand
    • Xiong JP, Stehle T, Zhang R, Joachimiak A, Frech M, Goodman SL, Arnaout MA. Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science 2002;296:151-155.
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 43
    • 0031571127 scopus 로고    scopus 로고
    • Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin
    • Carr PA, Erickson HP, Palmer AG III. Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin. Structure 1997;5:949-959.
    • (1997) Structure , vol.5 , pp. 949-959
    • Carr, P.A.1    Erickson, H.P.2    Palmer III, A.G.3
  • 44
    • 0036686104 scopus 로고    scopus 로고
    • Structural criteria of biologically active RGD-sites for analysis of protein cellular function: A bioinformatics study
    • Torshin IY. Structural criteria of biologically active RGD-sites for analysis of protein cellular function: a bioinformatics study. Med Sci Monit 2002;8:301-312.
    • (2002) Med Sci Monit , vol.8 , pp. 301-312
    • Torshin, I.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.