메뉴 건너뛰기




Volumn 13, Issue 4, 2007, Pages 269-279

The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif

Author keywords

Antimicrobial peptide; Inhibitory cystine knot (ICK) motif; Inmate immunity; NMR; Structure determination; Tachystatin B

Indexed keywords

ANTIBIOTIC AGENT; ARGININE; CHITIN; CYSTEINE; ION CHANNEL; POLYPEPTIDE ANTIBIOTIC AGENT; TACHYSTATIN A; TACHYSTATIN B; TACHYSTATIN B1; TACHYSTATIN B2; TYROSINE; UNCLASSIFIED DRUG;

EID: 34247351569     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.846     Document Type: Article
Times cited : (23)

References (51)
  • 2
    • 0034913684 scopus 로고    scopus 로고
    • Vertebrate innate immunity resembles a mosaic of invertebrate immune responses
    • Salzet M. Vertebrate innate immunity resembles a mosaic of invertebrate immune responses. Trends Immunol. 2001; 22: 285-288.
    • (2001) Trends Immunol , vol.22 , pp. 285-288
    • Salzet, M.1
  • 3
    • 5444234216 scopus 로고    scopus 로고
    • The interface between innate and adaptive immunity
    • Hoebe K, Jansen E, Beutler B. The interface between innate and adaptive immunity. Nat. Immunol. 2004; 5: 971-974.
    • (2004) Nat. Immunol , vol.5 , pp. 971-974
    • Hoebe, K.1    Jansen, E.2    Beutler, B.3
  • 4
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers JP. Hancock RE. The relationship between peptide structure and antibacterial activity. Peptides 2003; 24: 1681-1691.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 5
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • Dimarcq JL, Bulet P. Hetru C. Hoffmann J. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers 1999; 47: 465-477.
    • (1999) Biopolymers , vol.47 , pp. 465-477
    • Dimarcq, J.L.1    Bulet, P.2    Hetru, C.3    Hoffmann, J.4
  • 6
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 7
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik DJ, Daly NL, Waine C. The cystine knot motif in toxins and implications for drug design. Toxicon 2001; 39: 43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 8
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • Iwanaga S. Kawabata S, Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J. Biochem. (Tokyo) 1998; 123: 1-15.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 9
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga. S. The molecular basis of innate immunity in the horseshoe crab. Curr. Opin. Immunol. 2002; 14: 87-95.
    • (2002) Curr. Opin. Immunol , vol.14 , pp. 87-95
    • Iwanaga, S.1
  • 10
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga S, Lee BL. Recent advances in the innate immunity of invertebrate animals. J. Biochem. Mol. Biol. 2005; 38: 128-150.
    • (2005) J. Biochem. Mol. Biol , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 11
    • 0025989172 scopus 로고
    • Morphology of the granular hemocytes of the Japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances
    • Toh Y, Mizutani A, Tokunaga F, Muta T, Iwanaga. S. Morphology of the granular hemocytes of the Japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances. Cell Tissue Res. 1991; 266: 137-147.
    • (1991) Cell Tissue Res , vol.266 , pp. 137-147
    • Toh, Y.1    Mizutani, A.2    Tokunaga, F.3    Muta, T.4    Iwanaga, S.5
  • 12
    • 34247346651 scopus 로고    scopus 로고
    • Kawabata. S. Muta T. Iwanaga S. Clotting cascade and defense molecules found In the hemolymph of the horseshoe crab. In New Directions in Invertebrate Immunology, Söderhäll K. Iwanaga S. Vasta. GR (eds). SOS Publications: Fair Haven. NJ. 1996: 255-283.
    • Kawabata. S. Muta T. Iwanaga S. Clotting cascade and defense molecules found In the hemolymph of the horseshoe crab. In New Directions in Invertebrate Immunology, Söderhäll K. Iwanaga S. Vasta. GR (eds). SOS Publications: Fair Haven. NJ. 1996: 255-283.
  • 13
    • 0029928757 scopus 로고    scopus 로고
    • The role of hemolymph coagulation in innate immunity
    • Muta T, Iwanaga S. The role of hemolymph coagulation in innate immunity. Curr. Opin. Immunol. 1996: 8: 41-47.
    • (1996) Curr. Opin. Immunol , vol.8 , pp. 41-47
    • Muta, T.1    Iwanaga, S.2
  • 14
    • 0033522446 scopus 로고    scopus 로고
    • Tachylectin-2: Crystal structure of a specific GlcNAc/GaINAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus
    • Beisel HG, Kawabata S, Iwanaga S, Huber R, Bode W. Tachylectin-2: crystal structure of a specific GlcNAc/GaINAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus. EMBO J. 1999: 18: 2313-2322.
    • (1999) EMBO J , vol.18 , pp. 2313-2322
    • Beisel, H.G.1    Kawabata, S.2    Iwanaga, S.3    Huber, R.4    Bode, W.5
  • 15
    • 0035923237 scopus 로고    scopus 로고
    • Kairies N, Beisel HG, Fuentes-Prior P, Tsuda R. Muta T, Iwanaga. S. Bode W, Huber R, Kawabata. S. The 2.0-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity, and the blood coagulation systems. Proc. Natl. Acad. Sci. U.S.A. 2001; 98: 13519-13524.
    • Kairies N, Beisel HG, Fuentes-Prior P, Tsuda R. Muta T, Iwanaga. S. Bode W, Huber R, Kawabata. S. The 2.0-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity, and the blood coagulation systems. Proc. Natl. Acad. Sci. U.S.A. 2001; 98: 13519-13524.
  • 16
    • 0030462561 scopus 로고    scopus 로고
    • Crystal structure of limulus coagulogen: The clotting protein from horseshoe crab, a structural homologue of nerve growth factor
    • Bergner A, Oganessyan V. Muta T, Iwanaga S. Typke D. Huber R. Bode W. Crystal structure of limulus coagulogen: the clotting protein from horseshoe crab, a structural homologue of nerve growth factor. EMBO J. 1996; 15: 6789-6797.
    • (1996) EMBO J , vol.15 , pp. 6789-6797
    • Bergner, A.1    Oganessyan, V.2    Muta, T.3    Iwanaga, S.4    Typke, D.5    Huber, R.6    Bode, W.7
  • 17
    • 0025078937 scopus 로고
    • Antimicrobial peptide, tachyplesin I. isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus)
    • Kawano K, Yoneya T, Miyata T, Yoshikawa K, Tokunaga F, Terada Y. Iwanaga S. Antimicrobial peptide, tachyplesin I. isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). J. Biol. Chem. 1990; 265: 15365-15367.
    • (1990) J. Biol. Chem , vol.265 , pp. 15365-15367
    • Kawano, K.1    Yoneya, T.2    Miyata, T.3    Yoshikawa, K.4    Tokunaga, F.5    Terada, Y.6    Iwanaga, S.7
  • 18
    • 0037108278 scopus 로고    scopus 로고
    • Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives
    • Laederach A, Andreotti AH, Fulton DB. Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives. Biochemistry 2002; 41: 12359-12368.
    • (2002) Biochemistry , vol.41 , pp. 12359-12368
    • Laederach, A.1    Andreotti, A.H.2    Fulton, D.B.3
  • 19
    • 0034674709 scopus 로고    scopus 로고
    • Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif
    • Suetake T, Tsuda S. Kawabata S. Miura K, Iwanaga S, Hikichi K, Nitta K, Kawano K. Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. J. Biol. Chem. 2000; 275: 17929-17932.
    • (2000) J. Biol. Chem , vol.275 , pp. 17929-17932
    • Suetake, T.1    Tsuda, S.2    Kawabata, S.3    Miura, K.4    Iwanaga, S.5    Hikichi, K.6    Nitta, K.7    Kawano, K.8
  • 22
    • 0023700978 scopus 로고    scopus 로고
    • Nakamura T, Furunaka H. Miyata T, Tokunaga. F, Muta T, Iwanaga S, Niwa M, Takao T, Shimonishi Y. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). J. Biol. Chem. 1988; 263: 16709-16713.
    • Nakamura T, Furunaka H. Miyata T, Tokunaga. F, Muta T, Iwanaga S, Niwa M, Takao T, Shimonishi Y. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). J. Biol. Chem. 1988; 263: 16709-16713.
  • 24
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler L. Ernst RR. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 1983: 53: 521-528.
    • (1983) J. Magn. Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 25
    • 5144233105 scopus 로고
    • MLEV- 17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A, Davis DG. MLEV- 17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 1985: 65: 355-360.
    • (1985) J. Magn. Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 26
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J, Meier BN, Bachmann P, Ernst RR Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 1979; 71: 4546-4553.
    • (1979) J. Chem. Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.N.2    Bachmann, P.3    Ernst, R.R.4
  • 27
    • 0026951903 scopus 로고
    • Gradient-taflored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenár V. Gradient-taflored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 1992; 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 30
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C. Xia TH, Billeter M, Güntert P, Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 1995; 6: 1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 32
    • 33845378213 scopus 로고
    • Two-dimensional correlation of connected NMR transitions
    • Griesingcr C. Sørensen OW, Ernst RR. Two-dimensional correlation of connected NMR transitions. J. Am. Chem. Soc. 1985; 107: 6394-6396.
    • (1985) J. Am. Chem. Soc , vol.107 , pp. 6394-6396
    • Griesingcr, C.1    Sørensen, O.W.2    Ernst, R.R.3
  • 33
    • 0000857723 scopus 로고    scopus 로고
    • Characterization of protein unfolding by NMR diffusion measurements
    • Jones JA, Wilkins DK. Smith LJ, Dobson CM. Characterization of protein unfolding by NMR diffusion measurements. J. Biomol. NMR 1997; 1O: 199-203.
    • (1997) J. Biomol. NMR , vol.1 O , pp. 199-203
    • Jones, J.A.1    Wilkins, D.K.2    Smith, L.J.3    Dobson, C.M.4
  • 34
    • 0033554852 scopus 로고    scopus 로고
    • Wilkins DK Grimshaw SB, Receveur V. Dobson CM, Jones JA, Smith LJ. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 1999; 38: 16424-16431.
    • Wilkins DK Grimshaw SB, Receveur V. Dobson CM, Jones JA, Smith LJ. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 1999; 38: 16424-16431.
  • 35
    • 58149362694 scopus 로고
    • An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulses
    • Wu DH, Chen AD, Johnson CS Jr. An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulses. J. Magn. Reson. 1995; 115: 260-264.
    • (1995) J. Magn. Reson , vol.115 , pp. 260-264
    • Wu, D.H.1    Chen, A.D.2    Johnson Jr., C.S.3
  • 36
    • 3543012707 scopus 로고    scopus 로고
    • Brünger AT, Adams PD, Clore GM, DeLano WL. Gros P. Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM Simonson T, Warren GL. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D 1998; 54: 905-921.
    • Brünger AT, Adams PD, Clore GM, DeLano WL. Gros P. Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM Simonson T, Warren GL. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D 1998; 54: 905-921.
  • 37
    • 0037040913 scopus 로고    scopus 로고
    • The solution structures of the human β-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus
    • Schibli DJ, Hunter HN, Aseyev V, Starner TD, Wiencek JM, McCray PB Jr. Tack BF, Vogel HJ. The solution structures of the human β-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. J. Biol. Chem. 2002: 277: 8279-8289.
    • (2002) J. Biol. Chem , vol.277 , pp. 8279-8289
    • Schibli, D.J.1    Hunter, H.N.2    Aseyev, V.3    Starner, T.D.4    Wiencek, J.M.5    McCray Jr., P.B.6    Tack, B.F.7    Vogel, H.J.8
  • 39
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 1996: 14: 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 40
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides
    • Pallaghy PK, Nielsen KJ, Craik DJ, Norton RS. A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides. Protein Sci. 1994; 3: 1833-1839.
    • (1994) Protein Sci , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 41
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion chabbel toxins and related polypeptides
    • Norton RS, Pallaghy PK. The cystine knot structure of ion chabbel toxins and related polypeptides. Toxicon 1998; 36: 1573-1583.
    • (1998) Toxicon , vol.36 , pp. 1573-1583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 42
    • 0022705194 scopus 로고
    • Calculation of the isoelectric points of polypeptides from the amino acid composition
    • Skoog B. Wichman A. Calculation of the isoelectric points of polypeptides from the amino acid composition. Trends Anal. Chem. 1986: 5: 82-83.
    • (1986) Trends Anal. Chem , vol.5 , pp. 82-83
    • Skoog, B.1    Wichman, A.2
  • 45
    • 0037066147 scopus 로고    scopus 로고
    • Solution structures of the cis- and trans-Pro30 isomers of a novel 38-residue toxin from the venom of Hadronyche infensa sp. that contains a cystine-knot motif within its four disulfide bonds
    • Rosengren KJ, Wilson D, Daly NL, Alewood PF, Craik DJ. Solution structures of the cis- and trans-Pro30 isomers of a novel 38-residue toxin from the venom of Hadronyche infensa sp. that contains a cystine-knot motif within its four disulfide bonds. Biochemistry 2002; 41: 3294-3301.
    • (2002) Biochemistry , vol.41 , pp. 3294-3301
    • Rosengren, K.J.1    Wilson, D.2    Daly, N.L.3    Alewood, P.F.4    Craik, D.J.5
  • 47
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sander C. Mapping the protein universe. Science 1996; 273: 595-602.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 48
    • 15744367514 scopus 로고    scopus 로고
    • Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
    • Vaaje-Kolstad G, Houston DR, Riemen AH, Eijsink VG, van Aalten DM. Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21. J. Biol. Chem. 2005; 280: 11313-11319.
    • (2005) J. Biol. Chem , vol.280 , pp. 11313-11319
    • Vaaje-Kolstad, G.1    Houston, D.R.2    Riemen, A.H.3    Eijsink, V.G.4    van Aalten, D.M.5
  • 49
    • 4444330868 scopus 로고    scopus 로고
    • Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides Oliver at an atomic resolution
    • Xiang Y, Huang RH, Liu XZ. Zhang Y, Wang DC. Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides Oliver at an atomic resolution. J. Struct. Biol. 2004: 148: 86-97.
    • (2004) J. Struct. Biol , vol.148 , pp. 86-97
    • Xiang, Y.1    Huang, R.H.2    Liu, X.Z.3    Zhang, Y.4    Wang, D.C.5
  • 50
    • 2442669152 scopus 로고    scopus 로고
    • Solution structure of Eucommia antifungal peptide: A novel structural model distinct with a five-disulfide motif
    • Huang RH. Xiang Y. Tu GZ, Zhang Y, Wang DC. Solution structure of Eucommia antifungal peptide: a novel structural model distinct with a five-disulfide motif. Biochemistry 2004: 43: 6005-6012.
    • (2004) Biochemistry , vol.43 , pp. 6005-6012
    • Huang, R.H.1    Xiang, Y.T.G.2    Zhang, Y.3    Wang, D.C.4
  • 51
    • 0033529942 scopus 로고    scopus 로고
    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cysteine-knot disulfides
    • Tam JP, Lu YA, Yang JL. Chiu KW. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cysteine-knot disulfides. Proc. Natl. Acad. Sci. U.S.A. 1999: 96: 8913-8918.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 8913-8918
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3    Chiu, K.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.