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Volumn 44, Issue SUPPL. 1, 1997, Pages

Comparison of protein structures using 3D profile alignment

Author keywords

3D profile alignment; Evolution of protein structure; Protein structure comparison

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; EVOLUTION; GENE STRUCTURE; HEMOGLOBIN ANALYSIS; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0031028657     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00000065     Document Type: Article
Times cited : (25)

References (35)
  • 1
    • 0003338119 scopus 로고
    • Extracellular protein modules: A proposed nomenclature
    • poster CO2
    • Bork P, Bairoch A (1995) Extracellular protein modules: a proposed nomenclature. Trends Biochem Sci 20:poster CO2
    • (1995) Trends Biochem Sci , vol.20
    • Bork, P.1    Bairoch, A.2
  • 2
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork P, Sunder C, Valencia A (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci USA 89:7290-7294
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sunder, C.2    Valencia, A.3
  • 4
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie JU, Lüthy R, Eisenberg D (1991) A method to identify protein sequences that fold into a known three-dimensional structure. Science 253:164-170
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Lüthy, R.2    Eisenberg, D.3
  • 5
    • 0029008017 scopus 로고
    • Statistics of sequence - Structure threading
    • Bryant SH, Altschul SF (1995) Statistics of sequence - structure threading. Curr Opin Struct Biol 5:236-244
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 236-244
    • Bryant, S.H.1    Altschul, S.F.2
  • 6
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
    • Flaherty KM, McKay DB, Kabsch W, Holmes KC (1991) Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc Natl Acad Sci USA 88:5041-5045
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1    McKay, D.B.2    Kabsch, W.3    Holmes, K.C.4
  • 7
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein M, Lesk AM, Chothia C (1994) Structural mechanisms for domain movements in proteins. Biochemistry 33:6739-6749
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 8
    • 0018263844 scopus 로고
    • Why genes in pieces?
    • Gilbert W (1978) Why genes in pieces? Nature 271:501
    • (1978) Nature , vol.271 , pp. 501
    • Gilbert, W.1
  • 9
    • 0019860994 scopus 로고
    • Correlation of DNA exonic regions with protein structural units in haemoglobin
    • Go M (1981) Correlation of DNA exonic regions with protein structural units in haemoglobin. Nature 291:90-92
    • (1981) Nature , vol.291 , pp. 90-92
    • Go, M.1
  • 10
    • 0027459747 scopus 로고
    • Structural alignment of globins, phycocyanins and colicin A
    • Holm L, Sander C (1993a) Structural alignment of globins, phycocyanins and colicin A. FEBS Lett 315:301-306
    • (1993) FEBS Lett , vol.315 , pp. 301-306
    • Holm, L.1    Sander, C.2
  • 11
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C (1993b) Protein structure comparison by alignment of distance matrices. J Mol Biol 233:123-138
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 12
    • 0028232955 scopus 로고
    • Searching protein structure databases has come of age
    • Holm L, Sander C (1994) Searching protein structure databases has come of age. Proteins 19:165-173
    • (1994) Proteins , vol.19 , pp. 165-173
    • Holm, L.1    Sander, C.2
  • 13
    • 0042549133 scopus 로고
    • Comparisons of protein structures
    • Johnson MS (1991) Comparisons of protein structures. Curr Opin Struct Biol 1:334-344
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 334-344
    • Johnson, M.S.1
  • 14
    • 0029881326 scopus 로고    scopus 로고
    • Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of Paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein
    • Jones DT, Moody CM, Uppenbrink J, Viles JH, Doyle PM, Harris CJ, Pearl LH, Sadler PJ, Thornton JM (1996) Towards meeting the Paracelsus Challenge: the design, synthesis, and characterization of Paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein. Proteins 24:502-513
    • (1996) Proteins , vol.24 , pp. 502-513
    • Jones, D.T.1    Moody, C.M.2    Uppenbrink, J.3    Viles, J.H.4    Doyle, P.M.5    Harris, C.J.6    Pearl, L.H.7    Sadler, P.J.8    Thornton, J.M.9
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0025997601 scopus 로고
    • Secondary structure-based profiles: Use of structure-conserving scoring tables in searching protein sequence databases for structural similarities
    • Lüthy R, McLachlan AD, Eisenberg D (1991) Secondary structure-based profiles: use of structure-conserving scoring tables in searching protein sequence databases for structural similarities. Proteins 10:229-239
    • (1991) Proteins , vol.10 , pp. 229-239
    • Lüthy, R.1    McLachlan, A.D.2    Eisenberg, D.3
  • 18
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy R, Bowie JU, Eisenberg D (1992) Assessment of protein models with three-dimensional profiles. Nature 356:83-85
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 19
    • 0028579433 scopus 로고
    • Protein structural similarities predicted by a sequence-structure compatibility method
    • Matsuo Y, Nishikawa K (1994) Protein structural similarities predicted by a sequence-structure compatibility method. Protein Sci 3:2055-2063
    • (1994) Protein Sci , vol.3 , pp. 2055-2063
    • Matsuo, Y.1    Nishikawa, K.2
  • 20
    • 0029083544 scopus 로고
    • Detection of protein 3D-1D compatibility characterized by the evaluation of side-chain packing and electrostatic interactions
    • Matsuo Y, Nakamura H, Nishikawa K (1995) Detection of protein 3D-1D compatibility characterized by the evaluation of side-chain packing and electrostatic interactions. J Biochem 118:137-148
    • (1995) J Biochem , vol.118 , pp. 137-148
    • Matsuo, Y.1    Nakamura, H.2    Nishikawa, K.3
  • 21
    • 0018350099 scopus 로고
    • Gene duplications in the structural evolution of chymotrypsin
    • McLachlan AD (1979) Gene duplications in the structural evolution of chymotrypsin. J Mol Biol 128:49-79
    • (1979) J Mol Biol , vol.128 , pp. 49-79
    • McLachlan, A.D.1
  • 22
    • 0029164708 scopus 로고
    • Seeking significance in three-dimensional protein structure comparisons
    • Mizuguchi K, Go N (1995) Seeking significance in three-dimensional protein structure comparisons. Curr Opin Struct Biol 5:377-382
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 377-382
    • Mizuguchi, K.1    Go, N.2
  • 23
    • 0026556882 scopus 로고
    • β-Trefoil fold: Patterns of structure and sequence in the Kunitz inhibitors interleukins-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 interleukins-1β and 1α and fibroblast growth factors. J Mol Biol 223:531-543
    • (1992) J Mol Biol , vol.223 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 24
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman SB, Wunsch CD (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 48:443-453
    • (1970) J Mol Biol , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 25
    • 0027504808 scopus 로고
    • Development of pseudoenergy potentials for assessing protein 3D-1D compatibility and detecting weak homologies
    • Nishikawa K, Matsuo Y (1993) Development of pseudoenergy potentials for assessing protein 3D-1D compatibility and detecting weak homologies. Protein Eng 6:811-820
    • (1993) Protein Eng , vol.6 , pp. 811-820
    • Nishikawa, K.1    Matsuo, Y.2
  • 26
    • 0028319318 scopus 로고
    • Classification of protein folds
    • Orengo C (1994) Classification of protein folds. Curr Opin Struct Biol 4:429-440
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 429-440
    • Orengo, C.1
  • 28
    • 0029003770 scopus 로고
    • Desk-top analysis of the structural stability of various point mutations introduced into ribonuclease H
    • Ota M, Kanaya S, Nishikawa K (1995) Desk-top analysis of the structural stability of various point mutations introduced into ribonuclease H. J Mol Biol 248:733-738
    • (1995) J Mol Biol , vol.248 , pp. 733-738
    • Ota, M.1    Kanaya, S.2    Nishikawa, K.3
  • 29
    • 0025026058 scopus 로고
    • Comparison of the structures of globins and phycocyanins: Evidence for revolutionary relationship
    • Pastore A, Lesk AM (1990) Comparison of the structures of globins and phycocyanins: evidence for revolutionary relationship. Proteins 8:133-155
    • (1990) Proteins , vol.8 , pp. 133-155
    • Pastore, A.1    Lesk, A.M.2
  • 30
    • 0000319698 scopus 로고
    • Atomic structures and function of periplasmic receptors for active transport and chemotaxis
    • Quiocho FA (1991) Atomic structures and function of periplasmic receptors for active transport and chemotaxis. Curr Opin Struct Biol 1:922-933
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 922-933
    • Quiocho, F.A.1
  • 31
    • 0025370165 scopus 로고
    • Quantitative organization of the known protein x-ray structures. I. Methods and short-length-scale results
    • Rackovsky S (1990) Quantitative organization of the known protein x-ray structures. I. Methods and short-length-scale results. Proteins 7:378-402
    • (1990) Proteins , vol.7 , pp. 378-402
    • Rackovsky, S.1
  • 32
    • 0029563695 scopus 로고
    • Are database-derived potentials valid for scoring both forward and inverted protein folding?
    • Rooman MJ, Wodak SJ (1995) Are database-derived potentials valid for scoring both forward and inverted protein folding? Protein Eng 8:849-858
    • (1995) Protein Eng , vol.8 , pp. 849-858
    • Rooman, M.J.1    Wodak, S.J.2
  • 33
    • 0024349252 scopus 로고
    • Protein structure alignment
    • Taylor WR, Orengo CA (1989) Protein structure alignment. J Mol Biol 208:1-22
    • (1989) J Mol Biol , vol.208 , pp. 1-22
    • Taylor, W.R.1    Orengo, C.A.2
  • 35
    • 0027325129 scopus 로고
    • Families and the structural relatedness among globular proteins
    • Yee DP, Dill KA (1993) Families and the structural relatedness among globular proteins. Protein Sci 2:884-899
    • (1993) Protein Sci , vol.2 , pp. 884-899
    • Yee, D.P.1    Dill, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.