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Volumn 280, Issue 3, 1998, Pages 475-484

Crystal structure of a human embryonic haemoglobin: The carbonmonoxy form of Gower II (α2ε2) haemoglobin at 2.9 Å resolution

Author keywords

Chloride effect; Crystallography; Embryonic Hb; Haemoglobin

Indexed keywords

CARBOXYHEMOGLOBIN; HEMOGLOBIN F;

EID: 0032540854     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1868     Document Type: Article
Times cited : (17)

References (43)
  • 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
  • 2
    • 0001688940 scopus 로고
    • Different effects of 2,3-diphosphoglycerate and adenosine triphosphate on the oxygen affinity of adult and foetal human haemoglobin
    • Bauer C., Ludwig I., Ludwig M. Different effects of 2,3-diphosphoglycerate and adenosine triphosphate on the oxygen affinity of adult and foetal human haemoglobin. Life Sci. 7:1968;1339
    • (1968) Life Sci. , vol.7 , pp. 1339
    • Bauer, C.1    Ludwig, I.2    Ludwig, M.3
  • 4
    • 0028286465 scopus 로고
    • Chloride masks effects of opposing positive charges in Hb a and Hb Hinsdale (β139 Asn→Lys) that can modulate cooperativity as well as oxygen affinity
    • Bonaventura C., Arumugam M., Cashon R., Bonaventura J., Moo-Penn W.F. Chloride masks effects of opposing positive charges in Hb A and Hb Hinsdale (β139 Asn→Lys) that can modulate cooperativity as well as oxygen affinity. J. Mol. Biol. 239:1994;561-568
    • (1994) J. Mol. Biol. , vol.239 , pp. 561-568
    • Bonaventura, C.1    Arumugam, M.2    Cashon, R.3    Bonaventura, J.4    Moo-Penn, W.F.5
  • 5
    • 0030775069 scopus 로고    scopus 로고
    • A two-state analysis of co-operative oxygen binding in the three human embryonic haemoglobins
    • Brittain T., Hofmann O.M., Watmough N.J., Greenwood C., Weber R.E. A two-state analysis of co-operative oxygen binding in the three human embryonic haemoglobins. Biochem. J. 326:1997;299-303
    • (1997) Biochem. J. , vol.326 , pp. 299-303
    • Brittain, T.1    Hofmann, O.M.2    Watmough, N.J.3    Greenwood, C.4    Weber, R.E.5
  • 6
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R-value a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 7
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger A.T., Kuriyan J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 235:1987;458-460
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 10
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 11
    • 0021683974 scopus 로고
    • The crystal structure of human deoxyhaemoglobin at 1.74 Å
    • Fermi G., Perutz M.F., Shaanan B., Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74 Å 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
  • 12
    • 0017379826 scopus 로고
    • Structure of human foetal deoxyhaemoglobin
    • Frier J.A., Perutz M.F. Structure of human foetal deoxyhaemoglobin. J. Mol. Biol. 112:1977;97-112
    • (1977) J. Mol. Biol. , vol.112 , pp. 97-112
    • Frier, J.A.1    Perutz, M.F.2
  • 13
    • 0029913591 scopus 로고    scopus 로고
    • Ligand binding kinetics and dissociation of the human embryonic haemoglobins
    • Hofmann O., Brittain T. Ligand binding kinetics and dissociation of the human embryonic haemoglobins. Biochem. J. 315:1996;65-70
    • (1996) Biochem. J. , vol.315 , pp. 65-70
    • Hofmann, O.1    Brittain, T.2
  • 14
    • 0028909845 scopus 로고
    • Allosteric modulation of oxygen binding to the three human embryonic haemoglobins
    • Hofmann O., Mould R., Brittain T. Allosteric modulation of oxygen binding to the three human embryonic haemoglobins. Biochem. J. 306:1995;367-370
    • (1995) Biochem. J. , vol.306 , pp. 367-370
    • Hofmann, O.1    Mould, R.2    Brittain, T.3
  • 15
    • 0029153385 scopus 로고
    • The chloride effect in the human embryonic haemoglobins
    • Hofmann O., Carrucan G., Robson N., Brittain T. The chloride effect in the human embryonic haemoglobins. Biochem. J. 309:1995;959-962
    • (1995) Biochem. J. , vol.309 , pp. 959-962
    • Hofmann, O.1    Carrucan, G.2    Robson, N.3    Brittain, T.4
  • 16
    • 0016658268 scopus 로고
    • Oxygen dissociation properties of human embryonic red cells
    • Huehns E.R., Farooqui A.M. Oxygen dissociation properties of human embryonic red cells. Nature. 254:1975;335-337
    • (1975) Nature , vol.254 , pp. 335-337
    • Huehns, E.R.1    Farooqui, A.M.2
  • 17
    • 0027498175 scopus 로고
    • The quaternary structure of carbonmonoxy hemoglobin Ypsilanti
    • Janin J., Wodak S.J. The quaternary structure of carbonmonoxy hemoglobin Ypsilanti. Proteins: Struct. Funct. Genet. 15:1993;1-4
    • (1993) Proteins: Struct. Funct. Genet. , vol.15 , pp. 1-4
    • Janin, J.1    Wodak, S.J.2
  • 18
    • 0001797984 scopus 로고
    • TOM: A graphics fitting program for macromolecules
    • D. Sayre. Oxford: Clarendon Press
    • Jones T.A. TOM a graphics fitting program for macromolecules. Sayre D. Computational Crystallography. 1982;303-317 Clarendon Press, Oxford
    • (1982) Computational Crystallography , pp. 303-317
    • Jones, T.A.1
  • 19
    • 0027937718 scopus 로고
    • Structure determination of aquomet porcine hemoglobin at 2.8 Å resolution
    • Katz D.S., White S.P., Huang W., Kumar R., Christianson D.W. Structure determination of aquomet porcine hemoglobin at 2.8 Å resolution. J. Mol. Biol. 244:1994;541-553
    • (1994) J. Mol. Biol. , vol.244 , pp. 541-553
    • Katz, D.S.1    White, S.P.2    Huang, W.3    Kumar, R.4    Christianson, D.W.5
  • 20
    • 0026695805 scopus 로고
    • High resolution X-ray study of deoxyhemoglobin Rothschild 37β Trp→Arg: A mutation that creates an intersubunit chloride-binding site
    • Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A. High resolution X-ray study of deoxyhemoglobin Rothschild 37β Trp→Arg a mutation that creates an intersubunit chloride-binding site. Biochemistry. 31:1992;4111-4121
    • (1992) Biochemistry , vol.31 , pp. 4111-4121
    • Kavanaugh, J.S.1    Rogers, P.H.2    Case, D.A.3    Arnone, A.4
  • 21
    • 0000122663 scopus 로고
    • Search designs for protein crystallization based on orthogonal arrays
    • Kingston R.L., Baker H.M., Baker E.N. Search designs for protein crystallization based on orthogonal arrays. Acta Crystallog. sect D. 50:1994;429-440
    • (1994) Acta Crystallog. Sect D , vol.50 , pp. 429-440
    • Kingston, R.L.1    Baker, H.M.2    Baker, E.N.3
  • 22
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R., MacArthur M., Moss D., Thornton J. PROCHECK a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 23
    • 0028204237 scopus 로고
    • Production of human embryonic haemoglobin (Gower II) in a yeast expression system
    • Mould R.M., Hofmann O.M., Brittain T. Production of human embryonic haemoglobin (Gower II) in a yeast expression system. Biochem. J. 298:1994;619-622
    • (1994) Biochem. J. , vol.298 , pp. 619-622
    • Mould, R.M.1    Hofmann, O.M.2    Brittain, T.3
  • 24
    • 84920325457 scopus 로고
    • AMORE: An automated package for molecular replacement
    • Navaza J. AMORE an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 25
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 26
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington, UK: SERC Daresbury Laboratory
    • Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Proceedings of the CCP4 Study Weekend. 1993;56-62 SERC Daresbury Laboratory, Warrington, UK
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 27
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu N.S., Read R.J. Improved structure refinement through maximum likelihood. Acta Crystallog. sect. A. 52:1996;659-668
    • (1996) Acta Crystallog. Sect. a , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 28
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz M.F. Stereochemistry of cooperative effects in haemoglobin. Nature. 228:1970;726-734
    • (1970) Nature , vol.228 , pp. 726-734
    • Perutz, M.F.1
  • 29
    • 0027453843 scopus 로고
    • A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin
    • Perutz M.F., Fermi G., Poyart C., Pagnier J., Kister J. A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. J. Mol. Biol. 233:1993;536-545
    • (1993) J. Mol. Biol. , vol.233 , pp. 536-545
    • Perutz, M.F.1    Fermi, G.2    Poyart, C.3    Pagnier, J.4    Kister, J.5
  • 30
    • 0028245286 scopus 로고
    • The chloride effect in human haemoglobin. a new kind of allosteric mechanism
    • Perutz M.F., Shih D.T., Williamson D. The chloride effect in human haemoglobin. A new kind of allosteric mechanism. J. Mol. Biol. 239:1994;555-560
    • (1994) J. Mol. Biol. , vol.239 , pp. 555-560
    • Perutz, M.F.1    Shih, D.T.2    Williamson, D.3
  • 31
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A. 42:1986;140-149
    • (1986) Acta Crystallog. Sect. a , vol.42 , pp. 140-149
    • Read, R.J.1
  • 32
    • 0030589052 scopus 로고    scopus 로고
    • Heme stability in the human embryonic hemoglobins
    • Robson N., Brittain T. Heme stability in the human embryonic hemoglobins. J. Inorg. Biochem. 64:1996;137-147
    • (1996) J. Inorg. Biochem. , vol.64 , pp. 137-147
    • Robson, N.1    Brittain, T.2
  • 35
    • 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;31-61
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-61
    • Shaanan, B.1
  • 36
    • 0026795182 scopus 로고
    • A third quaternary structure of human hemoglobin a at 1.7 Å resolution
    • Silva M.M., Rogers P.H., Arnone A. A third quaternary structure of human hemoglobin A at 1.7 Å resolution. J. Biol. Chem. 267:1992;17248-17256
    • (1992) J. Biol. Chem. , vol.267 , pp. 17248-17256
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 37
    • 0028269771 scopus 로고
    • Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary state
    • Smith F.R., Simmons K.C. Cyanomet human hemoglobin crystallized under physiological conditions exhibits the Y quaternary state. Proteins: Struct. Funct. Genet. 18:1994;295-300
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 295-300
    • Smith, F.R.1    Simmons, K.C.2
  • 38
    • 0025903710 scopus 로고
    • The mutation β99 Asp-Tyr stabilizes Y, a new composite quaternary state of human hemoglobin
    • Smith F.R., Lattman E.E., Carter C.W. The mutation β99 Asp-Tyr stabilizes Y, a new composite quaternary state of human hemoglobin. Proteins: Struct. Funct. Genet. 10:1991;81-91
    • (1991) Proteins: Struct. Funct. Genet. , vol.10 , pp. 81-91
    • Smith, F.R.1    Lattman, E.E.2    Carter, C.W.3
  • 39
    • 0027988868 scopus 로고
    • The T-to-R transformation in hemoglobin: A reevaluation
    • Srinivasan R., Rose G.D. The T-to-R transformation in hemoglobin a reevaluation. 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.D.2
  • 40
    • 0002518563 scopus 로고    scopus 로고
    • Knowledge-based B-factor restraints for the refinement of proteins
    • Tronrud D.E. Knowledge-based B-factor restraints for the refinement of proteins. J. Appl. Crystallog. 29:1996;100-104
    • (1996) J. Appl. Crystallog. , vol.29 , pp. 100-104
    • Tronrud, D.E.1
  • 41
    • 84913050729 scopus 로고
    • An efficient general-purpose least squares refinement program for macromolecular structures
    • Tronrud D.E., Ten Eyck L.F., Matthews B.W. An efficient general-purpose least squares refinement program for macromolecular structures. Acta Crystallog. sect. A. 43:1987;489-501
    • (1987) Acta Crystallog. Sect. a , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 42
    • 0014446545 scopus 로고
    • Different response to organic phosphates of human fetal and adult hemoglobins
    • Tyuma I., Shimizu K. Different response to organic phosphates of human fetal and adult hemoglobins. Arch. Biochem. Biophys. 129:1969;404-405
    • (1969) Arch. Biochem. Biophys. , vol.129 , pp. 404-405
    • Tyuma, I.1    Shimizu, K.2


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