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Volumn 7, Issue 11, 1998, Pages 2324-2330

Singular points of protein β-sheets

Author keywords

Active site; Catalytic triad; Singular point; Surface topology; barrel

Indexed keywords

PROTEIN;

EID: 0031734779     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071109     Document Type: Article
Times cited : (5)

References (26)
  • 3
    • 0027423053 scopus 로고
    • Identification, classification, and analysis of beta-bulges in proteins
    • Chan AWE, Hutchingson EG, Harris D, Thornton JM. 1993. Identification, classification, and analysis of beta-bulges in proteins. Protein Sci 2:1574-1590.
    • (1993) Protein Sci , vol.2 , pp. 1574-1590
    • Chan, A.W.E.1    Hutchingson, E.G.2    Harris, D.3    Thornton, J.M.4
  • 4
    • 0015914783 scopus 로고
    • Conformation of twisted β-pleated sheets in proteins
    • Chothia C. 1973. Conformation of twisted β-pleated sheets in proteins. J Mol Biol 75:295-302.
    • (1973) J Mol Biol , vol.75 , pp. 295-302
    • Chothia, C.1
  • 5
    • 0020485895 scopus 로고
    • Orthogonal packing of β-pleated sheets in proteins
    • Chothia C, Janin J. 1982. Orthogonal packing of β-pleated sheets in proteins. Biochem 21:3955-3965.
    • (1982) Biochem , vol.21 , pp. 3955-3965
    • Chothia, C.1    Janin, J.2
  • 6
    • 0024961618 scopus 로고
    • Energy of stabilization of the right-handed βαβ crossover in proteins
    • Chou KC, Nemethy G, Pottle M, Scheraga HA. 1989. Energy of stabilization of the right-handed βαβ crossover in proteins. J Mol Biol 205:241-249.
    • (1989) J Mol Biol , vol.205 , pp. 241-249
    • Chou, K.C.1    Nemethy, G.2    Pottle, M.3    Scheraga, H.A.4
  • 7
    • 0025284257 scopus 로고
    • The evolution of α/β barrel enzymes
    • Farber GK, Petsko GA. 1990. The evolution of α/β barrel enzymes. TIBS 15:228-234.
    • (1990) TIBS , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 8
    • 0004227669 scopus 로고
    • Cambridge, UK: Cambridge University Press
    • Griffiths HB. 1976. Surfaces. Cambridge, UK: Cambridge University Press.
    • (1976) Surfaces
    • Griffiths, H.B.1
  • 9
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U, Sander C. 1994. Enlarged representative set of protein structures. Protein Sci 3:522-524.
    • (1994) Protein Sci , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 10
    • 0027092678 scopus 로고
    • Selection of a representative set of structures from the Brookhaven Protein Data Bank
    • Hobohm U, Scharf M, Schneider R, Sander C. 1992. Selection of a representative set of structures from the Brookhaven Protein Data Bank. Protein Sci 1:409-417.
    • (1992) Protein Sci , vol.1 , pp. 409-417
    • Hobohm, U.1    Scharf, M.2    Schneider, R.3    Sander, C.4
  • 11
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 12
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24:946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 13
    • 0031282923 scopus 로고    scopus 로고
    • Is there a Möbius band in closed protein β-sheets?
    • Liu W. 1997. Is there a Möbius band in closed protein β-sheets? Protein Eng 10:1373-1377.
    • (1997) Protein Eng , vol.10 , pp. 1373-1377
    • Liu, W.1
  • 14
    • 0032579317 scopus 로고    scopus 로고
    • Shear numbers of protein β-barrels: Definition refinements and statistics
    • Liu W. 1998. Shear numbers of protein β-barrels: Definition refinements and statistics. J Mol Biol 275:541-545.
    • (1998) J Mol Biol , vol.275 , pp. 541-545
    • Liu, W.1
  • 15
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM. 1994. Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 16
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. 1995. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 17
    • 0026556882 scopus 로고
    • β-Trefoil fold: Patterns of structure and sequence in the kunitz inhibitors interleukines-1β and 1α and fibroblast growth factors
    • Murzin AG, Lesk AM, Chothia C. 1992. β-Trefoil fold: Patterns of structure and sequence in the kunitz inhibitors interleukines-1β and 1α and fibroblast growth factors. J Mol Biol 225:531-543.
    • (1992) J Mol Biol , vol.225 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 18
    • 0028330220 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins: II. The observed structures
    • Murzin AG, Lesk AM, Chothia C. 1994. Principles determining the structure of β-sheet barrels in proteins: II. The observed structures. J Mol Biol 236:138-1400.
    • (1994) J Mol Biol , vol.236 , pp. 138-1400
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 19
    • 0344037144 scopus 로고
    • Handedness of crossover connections in β sheets
    • Richardson JS. 1976. Handedness of crossover connections in β sheets. Proc Nat Acad Sci USA 75:2619-2623.
    • (1976) Proc Nat Acad Sci USA , vol.75 , pp. 2619-2623
    • Richardson, J.S.1
  • 20
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS. 1981. The anatomy and taxonomy of protein structure. Advan Protein Chem 54:167-339.
    • (1981) Advan Protein Chem , vol.54 , pp. 167-339
    • Richardson, J.S.1
  • 21
    • 0001257560 scopus 로고
    • The β-bulge: A common small unit of nonrepetitive protein structure
    • Richardson JS, Getzoff ED, Richardson DC. 1978. The β-bulge: A common small unit of nonrepetitive protein structure. Proc Nat Acad Sci USA 75:2574-2578.
    • (1978) Proc Nat Acad Sci USA , vol.75 , pp. 2574-2578
    • Richardson, J.S.1    Getzoff, E.D.2    Richardson, D.C.3
  • 24
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman JL, Harel M, Frolow F, Oefner CO, Goldman A, Toker L, Silman I. 1991. Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein. Science 255:872-879.
    • (1991) Science , vol.255 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.O.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 25
    • 0028256135 scopus 로고
    • Preliminary X-ray analysis of Escherichia coli GMP synthetase: Determination of anomalous scattering factors for a cysteinyl mercury derivative
    • Tesmer JJG, Stemmler TL, Penner-Harn JE, Davisson VJ, Smith JL. 1994. Preliminary X-ray analysis of Escherichia coli GMP synthetase: Determination of anomalous scattering factors for a cysteinyl mercury derivative. Proteins Struct Fund Genet 18:394-403.
    • (1994) Proteins Struct Fund Genet , vol.18 , pp. 394-403
    • Tesmer, J.J.G.1    Stemmler, T.L.2    Penner-Harn, J.E.3    Davisson, V.J.4    Smith, J.L.5
  • 26
    • 0030024963 scopus 로고    scopus 로고
    • The crystal structure of GMP synthetase reveals a novel catalytic triad and is structural paradigm for two enzyme families
    • Tesmer JJG, Klem TJ, Deras ML, Davisson VJ, Smith JL. 1996. The crystal structure of GMP synthetase reveals a novel catalytic triad and is structural paradigm for two enzyme families. Nature Struct Biol 3:74-86.
    • (1996) Nature Struct Biol , vol.3 , pp. 74-86
    • Tesmer, J.J.G.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.