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Volumn 270, Issue 4, 1997, Pages 598-615

Conformation-invariant structures of the α1β1 human hemoglobin dimer

Author keywords

Allostery; Conserved structural domains; Hemoglobin; Protein conformation

Indexed keywords

DEOXYHEMOGLOBIN; DIMER; HEME; HEMOGLOBIN; OXYHEMOGLOBIN;

EID: 0031586213     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1087     Document Type: Article
Times cited : (38)

References (19)
  • 1
    • 0018361151 scopus 로고
    • Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
    • Baldwin J., Chothia C. Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129:1979;175-220.
    • (1979) J. Mol. Biol. , vol.129 , pp. 175-220
    • Baldwin, J.1    Chothia, C.2
  • 4
    • 0021683974 scopus 로고
    • The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution
    • Fermi G., Perutz M. F., Shaanan B., Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175:1984;159-174.
    • (1984) J. Mol. Biol. , vol.175 , pp. 159-174
    • Fermi, G.1    Perutz, M.F.2    Shaanan, B.3    Fourme, R.4
  • 5
    • 0029565638 scopus 로고
    • Using a measure of structure variation to define a core for the globins
    • Gerstein M., Altman R. B. Using a measure of structure variation to define a core for the globins. CABIOS. 11:1995;633-644.
    • (1995) CABIOS , vol.11 , pp. 633-644
    • Gerstein, M.1    Altman, R.B.2
  • 6
    • 0029818019 scopus 로고    scopus 로고
    • The oxygen-binding intermediates of human hemoglobin: Evaluation of their contributions to cooperativity using zinc-containing hybrids
    • Huang Y., Doyle M. L., Ackers G. K. The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids. Biophys. J. 71:1996;2094-2105.
    • (1996) Biophys. J. , vol.71 , pp. 2094-2105
    • Huang, Y.1    Doyle, M.L.2    Ackers, G.K.3
  • 7
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallog. sect. A. 32:1976;922-923.
    • (1976) Acta Crystallog. Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 8
    • 12944249776 scopus 로고
    • A discussion of the solution for the best solution to relate two sets of vectors
    • Kabsch W. A discussion of the solution for the best solution to relate two sets of vectors. Acta Crystallog. sect. A. 34:1978;827-828.
    • (1978) Acta Crystallog. Sect. A , vol.34 , pp. 827-828
    • Kabsch, W.1
  • 10
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 11
    • 0002983224 scopus 로고
    • Three-dimensional pattern matching in protein structure analysis
    • Berlin: Springer-Verlag
    • Lesk A. M. Three-dimensional pattern matching in protein structure analysis. Combinatorial Pattern Matching. 1995;Springer-Verlag, Berlin.
    • (1995) Combinatorial Pattern Matching
    • Lesk, A.M.1
  • 12
    • 0026552930 scopus 로고
    • A new mode for heme-heme interactions in hemoglobin associated with distal perturbations
    • Levy A., Sharma V. S., Zhang L., Rifkind J. M. A new mode for heme-heme interactions in hemoglobin associated with distal perturbations. Biophys. J. 61:1992;750-755.
    • (1992) Biophys. J. , vol.61 , pp. 750-755
    • Levy, A.1    Sharma, V.S.2    Zhang, L.3    Rifkind, J.M.4
  • 15
    • 0019209443 scopus 로고
    • Structure and refinement of oxymyoglobin at 1.6 Å resolution
    • Phillips S. E. V. Structure and refinement of oxymyoglobin at 1.6 Å resolution. J. Mol. Biol. 142:1980;531-554.
    • (1980) J. Mol. Biol. , vol.142 , pp. 531-554
    • Phillips, S.E.V.1
  • 16
    • 0027993426 scopus 로고
    • Nanosecond dynamics of the R→T transition in hemoglobin: Ultraviolet raman studies
    • Rodgers K. R., Spiro T. G. Nanosecond dynamics of the R→T transition in hemoglobin: ultraviolet raman studies. Science. 265:1994;1697-1699.
    • (1994) Science , vol.265 , pp. 1697-1699
    • Rodgers, K.R.1    Spiro, T.G.2
  • 17
    • 0021027685 scopus 로고
    • Structure of human oxyhaemoglobin at 2.1 Å resolution
    • Shaanan B. Structure of human oxyhaemoglobin at 2.1 Å resolution. J. Mol. Biol. 171:1983;31-59.
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 18
    • 0027988868 scopus 로고
    • The T to R Transformation in hemoglobin: A re-evaluation
    • Srinivasan R., Rose G. The T to R Transformation in hemoglobin: a re-evaluation. Proc. Natl Acad. Sci. USA. 91:1994;11113-11117.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11113-11117
    • Srinivasan, R.1    Rose, G.2
  • 19
    • 0011076031 scopus 로고
    • Hemoglobin and myoglobin
    • D. Dolphin. San Diego: Academic Press
    • Ten Eyck L. F. Hemoglobin and myoglobin. Dolphin D. The Porphyrins. 1979;Academic Press, San Diego.
    • (1979) The Porphyrins
    • Ten Eyck, L.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.