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Volumn 39, Issue 2, 2000, Pages 142-154

Sequence and structural features of the T-fold, an original tunnelling building unit

Author keywords

Folding motif; Oligomeric assembly; Sequence divergence; Structural similarity; Topohydrophobic network

Indexed keywords

ARTICLE; BINDING SITE; ENZYME BINDING; ENZYME STRUCTURE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; SEQUENCE HOMOLOGY;

EID: 0034192571     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000501)39:2<142::AID-PROT4>3.0.CO;2-X     Document Type: Article
Times cited : (57)

References (42)
  • 1
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin AG. OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. Embo J 1993;12:861-867.
    • (1993) Embo J , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 2
    • 0032189646 scopus 로고    scopus 로고
    • Dictionary of recurrent domains in protein structures
    • Holm L, Sander C. Dictionary of recurrent domains in protein structures. Proteins 1998;33:88-96.
    • (1998) Proteins , vol.33 , pp. 88-96
    • Holm, L.1    Sander, C.2
  • 3
    • 0031815861 scopus 로고    scopus 로고
    • A re-estimation for the total numbers of protein folds and superfamilies
    • Wang ZX. A re-estimation for the total numbers of protein folds and superfamilies. Protein Eng 1998;11:621-626.
    • (1998) Protein Eng , vol.11 , pp. 621-626
    • Wang, Z.X.1
  • 4
    • 0032545151 scopus 로고    scopus 로고
    • Estimating the number of protein folds
    • Zhang C, DeLisi C. Estimating the number of protein folds. J Mol Biol 1998;284:1301-1305.
    • (1998) J Mol Biol , vol.284 , pp. 1301-1305
    • Zhang, C.1    DeLisi, C.2
  • 8
    • 0030663655 scopus 로고    scopus 로고
    • Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution
    • Colloc'h N, El Hajji M, Bachet B, et al. Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution. Nat Struct Biol 1997;4:947-952.
    • (1997) Nat Struct Biol , vol.4 , pp. 947-952
    • Colloc'h, N.1    El Hajji, M.2    Bachet, B.3
  • 9
    • 0017411710 scopus 로고
    • The protein data bank: A computer based archival file for macromolecular structures
    • Bernstein FC, Koetzle TF, Williams GJB, et al. The protein data bank: a computer based archival file for macromolecular structures. J Mol Biol 1977;112:535-542.
    • (1977) J Mol Biol , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Koetzle, T.F.2    Williams, G.J.B.3
  • 10
    • 0032893084 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999
    • Bairoch A, Apweiler R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999. Nucleic Acids Res 1999;27:49-54.
    • (1999) Nucleic Acids Res , vol.27 , pp. 49-54
    • Bairoch, A.1    Apweiler, R.2
  • 11
    • 0030998184 scopus 로고    scopus 로고
    • P-SEA: A new efficient assignment of secondary structure from C a trace of proteins
    • Labesse G, Colloc'h N, Pothier J, Mornon JP. P-SEA: a new efficient assignment of secondary structure from C a trace of proteins. Comput Appl Biosci 1997;13:291-295.
    • (1997) Comput Appl Biosci , vol.13 , pp. 291-295
    • Labesse, G.1    Colloc'h, N.2    Pothier, J.3    Mornon, J.P.4
  • 12
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 13
    • 0032534020 scopus 로고    scopus 로고
    • Populations of hydrophobic amino acids within protein globular domains: Identification of conserved "topohydrophobic" positions
    • Poupon A, Mornon JP. Populations of hydrophobic amino acids within protein globular domains: identification of conserved "topohydrophobic" positions. Proteins 1998;33:329-342.
    • (1998) Proteins , vol.33 , pp. 329-342
    • Poupon, A.1    Mornon, J.P.2
  • 14
    • 0028264849 scopus 로고
    • Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis
    • Nar H, Huber R, Heizmann CW, Thony B, Burgisser D. Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis. Embo J 1994;13:1255-1262.
    • (1994) Embo J , vol.13 , pp. 1255-1262
    • Nar, H.1    Huber, R.2    Heizmann, C.W.3    Thony, B.4    Burgisser, D.5
  • 15
    • 0028971611 scopus 로고
    • 6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding
    • Burgisser DM, Thony B, Redweik U, et al. 6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding. J Mol Biol 1995;253:358-369.
    • (1995) J Mol Biol , vol.253 , pp. 358-369
    • Burgisser, D.M.1    Thony, B.2    Redweik, U.3
  • 16
    • 0032066057 scopus 로고    scopus 로고
    • Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus
    • Hennig M, D'Arcy A, Hampele IC, Page MG, Oefner C, Dale GE. Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus. Nat Struct Biol 1998;5: 357-362.
    • (1998) Nat Struct Biol , vol.5 , pp. 357-362
    • Hennig, M.1    D'Arcy, A.2    Hampele, I.C.3    Page, M.G.4    Oefner, C.5    Dale, G.E.6
  • 19
    • 13344259317 scopus 로고
    • Active site topology and reaction mechanism of GTP cyclohydrolase I
    • Nar H, Huber R, Auerbach G, et al. Active site topology and reaction mechanism of GTP cyclohydrolase I. Proc Natl Acad Sci USA 1995;92:12120-12125.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12120-12125
    • Nar, H.1    Huber, R.2    Auerbach, G.3
  • 20
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 1991;349: 117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 22
    • 0033461553 scopus 로고    scopus 로고
    • "Topohydrophobic positions" as key markers of globular protein folds
    • Poupon A, Mornon JP. "Topohydrophobic positions" as key markers of globular protein folds. Theor Chem Acc 1999;101:2-8.
    • (1999) Theor Chem Acc , vol.101 , pp. 2-8
    • Poupon, A.1    Mornon, J.P.2
  • 23
    • 0033004893 scopus 로고    scopus 로고
    • Predicting the protein folding nucleus from sequences
    • published errata; 457: 525
    • Poupon A, Mornon JP. Predicting the protein folding nucleus from sequences. FEBS Lett 1999; 452:283-289 (published errata; 457: 525).
    • (1999) FEBS Lett , vol.452 , pp. 283-289
    • Poupon, A.1    Mornon, J.P.2
  • 25
    • 0030690133 scopus 로고    scopus 로고
    • Deciphering protein sequence information through hydrophobic cluster analysis (HCA): Current status and perspectives
    • Callebaut I, Labesse G, Durand P, et al. Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cell Mol Life Sci 1997;53:621-645.
    • (1997) Cell Mol Life Sci , vol.53 , pp. 621-645
    • Callebaut, I.1    Labesse, G.2    Durand, P.3
  • 26
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR. Profile hidden Markov models. Bioinformatics 1998;14; 755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 27
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sander C. Mapping the protein universe. Science 1996;273: 595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 28
    • 0029950832 scopus 로고    scopus 로고
    • Understanding protein structure: Using scop for fold interpretation
    • Brenner SE, Chothia C, Hubbard TJ, Murzin AG. Understanding protein structure: using scop for fold interpretation. Methods Enzymol 1996;266:635-643.
    • (1996) Methods Enzymol , vol.266 , pp. 635-643
    • Brenner, S.E.1    Chothia, C.2    Hubbard, T.J.3    Murzin, A.G.4
  • 31
    • 0030988695 scopus 로고    scopus 로고
    • Two new examples of protein structural similarities within the structure-function twilight zone
    • Russell RB, Sternberg MJ. Two new examples of protein structural similarities within the structure-function twilight zone. Protein Eng 1997;10:333-338.
    • (1997) Protein Eng , vol.10 , pp. 333-338
    • Russell, R.B.1    Sternberg, M.J.2
  • 32
    • 0029137828 scopus 로고
    • The structure and evolution of α/beta barrel proteins
    • Reardon D, Farber GK. The structure and evolution of α/beta barrel proteins. Faseb J 1995;9:497-503.
    • (1995) Faseb J , vol.9 , pp. 497-503
    • Reardon, D.1    Farber, G.K.2
  • 33
    • 0031302793 scopus 로고    scopus 로고
    • Distant homology recognition using structural classification of proteins
    • Murzin AG, Bateman A. Distant homology recognition using structural classification of proteins. Proteins 1997;Suppl 1:105-112.
    • (1997) Proteins , Issue.1 SUPPL. , pp. 105-112
    • Murzin, A.G.1    Bateman, A.2
  • 34
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • Orengo CA, Jones DT, Thornton JM. Protein superfamilies and domain superfolds. Nature 1994;372:631-634.
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 35
    • 0027122441 scopus 로고
    • Familiar strangers
    • Murzin AG. Familiar strangers. Nature 1992;360:635.
    • (1992) Nature , vol.360 , pp. 635
    • Murzin, A.G.1
  • 36
    • 0032104477 scopus 로고    scopus 로고
    • How far divergent evolution goes in proteins
    • Murzin AG. How far divergent evolution goes in proteins. Curr Opin Struct Biol 1998;8:380-387.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 380-387
    • Murzin, A.G.1
  • 37
    • 0026556882 scopus 로고
    • Beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 a and fibroblast growth factors
    • Murzin AG, Lesk AM, Chothia C. Beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 a and fibroblast growth factors. J Mol Biol 1992;223:531-543.
    • (1992) J Mol Biol , vol.223 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 38
    • 0032927791 scopus 로고    scopus 로고
    • Folding by association
    • Shakhnovich EI. Folding by association. Nat Struct Biol 1999;6:99-102.
    • (1999) Nat Struct Biol , vol.6 , pp. 99-102
    • Shakhnovich, E.I.1
  • 39
    • 0032906377 scopus 로고    scopus 로고
    • Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53
    • Mateu MG, Sanchez Del Pino MM, Fersht AR. Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53. Nat Struct Biol 1999;6:191-198.
    • (1999) Nat Struct Biol , vol.6 , pp. 191-198
    • Mateu, M.G.1    Sanchez Del Pino, M.M.2    Fersht, A.R.3
  • 40
    • 0027482006 scopus 로고
    • Human CksHs2 atomic structure: A role for its hexameric assembly in cell cycle control
    • Parge HE, Arvai AS, Murtari DJ, Reed SI, Tainer JA. Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control. Science 1993;262:387-394
    • (1993) Science , vol.262 , pp. 387-394
    • Parge, H.E.1    Arvai, A.S.2    Murtari, D.J.3    Reed, S.I.4    Tainer, J.A.5
  • 41
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J Appl Crystallogr 1991;24: 946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 42
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Multiple sequence alignments in Postscript
    • Gouet P, Courcelle E, Stuart D, Metoz F. ESPript: multiple sequence alignments in Postscript. Bioinformatics 1999;15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.3    Metoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.