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Volumn 9, Issue 11-12, 2003, Pages 769-775

The peptaibol antiamoebin as a model ion channel: Similarities to bacterial potassium channels

Author keywords

Alamethicin; Conductance; Crystal structure; Ion channel; Molecular model; Potassium channel

Indexed keywords

ALAMETHICIN; ANTIAMEBIC AGENT; ION CHANNEL; PEPTAIBOL; POTASSIUM CHANNEL; POTASSIUM ION; TRICHOTOXIN; UNCLASSIFIED DRUG;

EID: 0344739801     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.514     Document Type: Article
Times cited : (17)

References (31)
  • 1
    • 0014232472 scopus 로고
    • Antiamoebin, a new antiprotozoal-antihelmintic antibiotic. Part I. Production and biological studies
    • Thirumalachur MJ. Antiamoebin, a new antiprotozoal-antihelmintic antibiotic. Part I. Production and biological studies. Hindustan Antibiotic Bull. 1968; 10: 287-289.
    • (1968) Hindustan Antibiotic Bull. , vol.10 , pp. 287-289
    • Thirumalachur, M.J.1
  • 2
    • 0032466175 scopus 로고    scopus 로고
    • Antiamoebin can function as a carrier or as a pore-forming peptaibol
    • 1415
    • Duclohier H, Snook CF, Wallace BA. Antiamoebin can function as a carrier or as a pore-forming peptaibol. Biochim. Biophys. Acta 1998; 1415: 255-260.
    • (1998) Biochim. Biophys. Acta , pp. 255-260
    • Duclohier, H.1    Snook, C.F.2    Wallace, B.A.3
  • 3
    • 0021158372 scopus 로고
    • The stereochemistry of peptides containing alpha-aminoisobutyric acid
    • Prasad BV, Balaram P. The stereochemistry of peptides containing alpha-aminoisobutyric acid. CRC Crit. Rev. Biochem. 1984; 16: 307-347.
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 307-347
    • Prasad, B.V.1    Balaram, P.2
  • 4
    • 0016183539 scopus 로고
    • Statistical analysis of alamethicin channels in black lipid membranes
    • Boheim G. Statistical analysis of alamethicin channels in black lipid membranes. J. Membr. Biol. 1974; 19: 277-303.
    • (1974) J. Membr. Biol. , vol.19 , pp. 277-303
    • Boheim, G.1
  • 5
    • 0023754246 scopus 로고
    • Conformation of alamethicin in phospholipid vesicles: Implications for insertion models
    • Cascio M, Wallace BA. Conformation of alamethicin in phospholipid vesicles: implications for insertion models. Proteins: Struct. Funct. Genet. 1988; 4: 89-98.
    • (1988) Proteins: Struct. Funct. Genet. , vol.4 , pp. 89-98
    • Cascio, M.1    Wallace, B.A.2
  • 6
    • 0028226051 scopus 로고
    • Alamethicin - A peptide model for voltage gating and protein-membrane interactions
    • Cafiso DS. Alamethicin - a peptide model for voltage gating and protein-membrane interactions. Ann. Rev. Biophys. Biomol. Struct. 1994; 23: 141-165.
    • (1994) Ann. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 141-165
    • Cafiso, D.S.1
  • 10
    • 0020360086 scopus 로고
    • A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5 Å resolution
    • Fox RO, Jr, Richards FM. A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5 Å resolution. Nature 1982; 300: 325-330.
    • (1982) Nature , vol.300 , pp. 325-330
    • Fox Jr., R.O.1    Richards, F.M.2
  • 11
    • 0032510799 scopus 로고    scopus 로고
    • Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment
    • Karle IL, Perozzo MA, Mishra VK, Balaram P. Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment. Proc. Natl Acad. Sci. USA 1998; 95: 5501-5504.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5501-5504
    • Karle, I.L.1    Perozzo, M.A.2    Mishra, V.K.3    Balaram, P.4
  • 12
    • 0025924739 scopus 로고
    • Crystal structure of [Leu1]-zervamicin, a membrane ion-channel peptide: Implications for gating mechanisms
    • Karle IL, Flippen-Anderson JL, Agarwalla S, Balaram P. Crystal structure of [Leu1]-zervamicin, a membrane ion-channel peptide: implications for gating mechanisms. Proc. Natl Acad. Sci. USA 1991; 88: 5307-5311.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5307-5311
    • Karle, I.L.1    Flippen-Anderson, J.L.2    Agarwalla, S.3    Balaram, P.4
  • 13
    • 0037195259 scopus 로고    scopus 로고
    • Model for a helical bundle channel based on the high resolution crystal structure of trichotoxin0E
    • Chugh JK, Brückner H, Wallace BA. Model for a helical bundle channel based on the high resolution crystal structure of trichotoxin0E. Biochemistry 2002; 41: 12934-12941.
    • (2002) Biochemistry , vol.41 , pp. 12934-12941
    • Chugh, J.K.1    Brückner, H.2    Wallace, B.A.3
  • 14
    • 0025935264 scopus 로고
    • The biophysics of peptide models of ion channels
    • Sansom MSP. The biophysics of peptide models of ion channels. Prog. Biophys. Mol. Biol. 1991; 55: 139-156.
    • (1991) Prog. Biophys. Mol. Biol. , vol.55 , pp. 139-156
    • Sansom, M.S.P.1
  • 15
    • 0034013154 scopus 로고    scopus 로고
    • Common structural features in gramicidin and other ion channels
    • Wallace BA. Common structural features in gramicidin and other ion channels. Bioessays 2000; 22: 227-234.
    • (2000) Bioessays , vol.22 , pp. 227-234
    • Wallace, B.A.1
  • 16
    • 0345148576 scopus 로고
    • SYBYL, version 6.8, Tripos Inc., South Hanley Rd., St Louis, MO, USA
    • SYBYL, version 6.8, Tripos Inc., 1699 South Hanley Rd., St Louis, MO, USA.
    • (1699)
  • 17
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 Suite: programs for protein crystallography. Acta Cryst. 1994; D50: 760-763.
    • (1994) Acta Cryst. , vol.D50 , pp. 760-763
  • 18
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 1971; 55: 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 19
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 1991; 11: 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 20
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • Smart OS, Neduvelil JG, Wang X, Wallace BA, Sansom MSP. HOLE: A program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graphics 1996; 14: 354-360.
    • (1996) J. Mol. Graphics , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.P.5
  • 22
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 2002; 417: 515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 23
    • 0033198356 scopus 로고    scopus 로고
    • The molecular replacement solution of an intermediate-sized helical polypeptide, antiamoebin I
    • Snook CF, Wallace BA. The molecular replacement solution of an intermediate-sized helical polypeptide, antiamoebin I. Acta Cryst. 1999; D55: 1539-1545.
    • (1999) Acta Cryst. , vol.D55 , pp. 1539-1545
    • Snook, C.F.1    Wallace, B.A.2
  • 25
    • 0023726958 scopus 로고
    • Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain
    • Sali D, Bycroft M, Fersht AR. Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain. Nature 1988; 335: 740-743.
    • (1988) Nature , vol.335 , pp. 740-743
    • Sali, D.1    Bycroft, M.2    Fersht, A.R.3
  • 26
    • 0034467939 scopus 로고    scopus 로고
    • Tryptophans in membrane proteins: X-ray crystallographic analyses
    • Wallace BA, Janes RW. Tryptophans in membrane proteins: x-ray crystallographic analyses. Adv. Exp. Med. Biol. 1999; 467: 789-799.
    • (1999) Adv. Exp. Med. Biol. , vol.467 , pp. 789-799
    • Wallace, B.A.1    Janes, R.W.2
  • 27
    • 0016586549 scopus 로고
    • Ion-membrane interactions as structural forces
    • Parsegian VA. Ion-membrane interactions as structural forces. Ann. NY Acad. Sci. 1975; 264: 161-171.
    • (1975) Ann. NY Acad. Sci. , vol.264 , pp. 161-171
    • Parsegian, V.A.1
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 1991; 24: 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt EA, Bacon DJ. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 1997; 277: 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.