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Volumn 256, Issue 4, 1996, Pages 775-792

Crystal structure of T state haemoglobin with oxygen bound at all four haems

Author keywords

Cooperativity; Crystallography; Haemoglobin; Oxygenation; T state

Indexed keywords

HEME; HEMOGLOBIN; OXYGEN; OXYHEMOGLOBIN;

EID: 0030000410     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0124     Document Type: Article
Times cited : (163)

References (27)
  • 1
    • 0026671889 scopus 로고
    • X-ray diffraction study of di and tetra-ligated T-state haemoglobin from high salt crystals
    • Abraham, D. J., Peascoe, R. A., Randad, R. S. & Panikker, J. (1992). X-ray diffraction study of di and tetra-ligated T-state haemoglobin from high salt crystals. J. Biol. Chem. 227, 480-492.
    • (1992) J. Biol. Chem. , vol.227 , pp. 480-492
    • Abraham, D.J.1    Peascoe, R.A.2    Randad, R.S.3    Panikker, J.4
  • 2
    • 0015908917 scopus 로고
    • Intermediate structure of normal human haemoglobin: Methaemoglobin in the deoxy quaternary conformation
    • Anderson, L. (1973). Intermediate structure of normal human haemoglobin: methaemoglobin in the deoxy quaternary conformation. J. Mol. Biol. 79, 495-506.
    • (1973) J. Mol. Biol. , vol.79 , pp. 495-506
    • Anderson, L.1
  • 3
    • 0018361151 scopus 로고
    • Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
    • Baldwin, J. & Chothia, C. (1979). Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129, 175-220.
    • (1979) J. Mol. Biol. , vol.129 , pp. 175-220
    • Baldwin, J.1    Chothia, C.2
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (1994). The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 9
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, A. (1978). A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11, 268-272.
    • (1978) J. Appl. Crystallog. , vol.11 , pp. 268-272
    • Jones, A.1
  • 10
    • 0015101813 scopus 로고
    • The binding of carbon dioxide by horse haemoglobin
    • Kilmartin, J. V. & Rossi-Bernardi, L. (1971). The binding of carbon dioxide by horse haemoglobin. Biochem. J. 124, 31-45.
    • (1971) Biochem. J. , vol.124 , pp. 31-45
    • Kilmartin, J.V.1    Rossi-Bernardi, L.2
  • 11
    • 0001720577 scopus 로고
    • A restrained parameter thermal factor refinement procedure
    • Konnert, J. & Hendrickson, W. (1980). A restrained parameter thermal factor refinement procedure. Acta Crystallog. sect. A, 36, 344-350.
    • (1980) Acta Crystallog. Sect. A , vol.36 , pp. 344-350
    • Konnert, J.1    Hendrickson, W.2
  • 13
    • 0023876537 scopus 로고
    • Structure of the liganded T state of haemoglobin identifies the origins of cooperative oxygen binding
    • Liddington, R. C., Derewenda, Z., Dodson, G. & Harris, D. (1988). Structure of the liganded T state of haemoglobin identifies the origins of cooperative oxygen binding. Nature, 331, 725-728.
    • (1988) Nature , vol.331 , pp. 725-728
    • Liddington, R.C.1    Derewenda, Z.2    Dodson, G.3    Harris, D.4
  • 14
    • 0026620795 scopus 로고
    • High resolution crystal structures and comparisons of T state deoxy and two liganded T state haemoglobins: T (α-oxy) haemoglobin and T (met) haemoglobin
    • Liddington, R. C., Derewenda, Z., Dodson, G., Dodson, E., Hubbard, R. & Dodson, G. (1992). High resolution crystal structures and comparisons of T state deoxy and two liganded T state haemoglobins: T (α-oxy) haemoglobin and T (met) haemoglobin. J. Mol. Biol. 228, 551-579.
    • (1992) J. Mol. Biol. , vol.228 , pp. 551-579
    • Liddington, R.C.1    Derewenda, Z.2    Dodson, G.3    Dodson, E.4    Hubbard, R.5    Dodson, G.6
  • 16
    • 0025299882 scopus 로고
    • Structure of deoxy quaternary haemoglobin with liganded β subunits
    • Luisi, B., Liddington, R., Fermi, G. & Shibayama, N. (1990). Structure of deoxy quaternary haemoglobin with liganded β subunits. J. Mol. Biol. 214, 7-14.
    • (1990) J. Mol. Biol. , vol.214 , pp. 7-14
    • Luisi, B.1    Liddington, R.2    Fermi, G.3    Shibayama, N.4
  • 17
    • 0024281313 scopus 로고
    • T-state haemoglobin with four ligands bound
    • Marden, M. C., Kister, J., Bohn, B. & Poyart, C. (1988). T-state haemoglobin with four ligands bound. Biochemistry, 27, 1659-1664.
    • (1988) Biochemistry , vol.27 , pp. 1659-1664
    • Marden, M.C.1    Kister, J.2    Bohn, B.3    Poyart, C.4
  • 18
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. & Changeux, J.-P. (1965). On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 19
    • 0025801633 scopus 로고
    • Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect
    • Mozzarelli, A., Rivetti, C., Rossi, G. L., Henry, E. R. & Eaton, W. A. (1990). Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect. Nature, 351, 416-419.
    • (1990) Nature , vol.351 , pp. 416-419
    • Mozzarelli, A.1    Rivetti, C.2    Rossi, G.L.3    Henry, E.R.4    Eaton, W.A.5
  • 20
    • 0001793063 scopus 로고
    • Preparation of haemoglobin crystals
    • Perutz, M. F. (1968). Preparation of haemoglobin crystals. J. Crystal Growth, 2, 54-56.
    • (1968) J. Crystal Growth , vol.2 , pp. 54-56
    • Perutz, M.F.1
  • 21
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz, M. F. (1970). Stereochemistry of cooperative effects in haemoglobin. Nature, 228, 226-233.
    • (1970) Nature , vol.228 , pp. 226-233
    • Perutz, M.F.1
  • 22
    • 0015529611 scopus 로고
    • Haem-haem interaction
    • Perutz, M. F. (1972). Haem-haem interaction. Nature, 237, 495-499.
    • (1972) Nature , vol.237 , pp. 495-499
    • Perutz, M.F.1
  • 25
    • 0021027685 scopus 로고
    • Structure of oxyhaemoglobin at 2.1 Å resolution
    • Shaanan, B. (1983). Structure of oxyhaemoglobin at 2.1 Å resolution. J. Mol. Biol. 171, 31-59.
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 26
    • 0029062547 scopus 로고
    • Allosteric transition intermediates modelled by crosslinked haemoglobins
    • Shumaker, M. A., Dixon, M. M., Kluger, R., Jones, R. T. & Brennan, R. G. (1995). Allosteric transition intermediates modelled by crosslinked haemoglobins. Nature, 375, 84-87.
    • (1995) Nature , vol.375 , pp. 84-87
    • Shumaker, M.A.1    Dixon, M.M.2    Kluger, R.3    Jones, R.T.4    Brennan, R.G.5
  • 27
    • 0016824616 scopus 로고
    • Structure of deoxyhaemoglobin A crystals grown from polyethylene glycol solutions
    • Ward, K. B., Wishner, B. C., Lattman, E. & Lowe, W. E. (1975). Structure of deoxyhaemoglobin A crystals grown from polyethylene glycol solutions. J. Mol. Biol. 98, 161-179.
    • (1975) J. Mol. Biol. , vol.98 , pp. 161-179
    • Ward, K.B.1    Wishner, B.C.2    Lattman, E.3    Lowe, W.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.