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Volumn 398, Issue 1-2 SPEC. ISS., 2007, Pages 29-34

Crystal structures of two hemoglobin components from the midge larva Propsilocerus akamusi (Orthocladiinae, Diptera)

Author keywords

Additional helix; Amino acid replacement; Distal histidine; Insect hemoglobin; X ray crystallography

Indexed keywords

AMINO ACID; HEMOGLOBIN; HISTIDINE; ISOLEUCINE;

EID: 34447559436     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2007.02.049     Document Type: Article
Times cited : (5)

References (19)
  • 1
    • 0028308355 scopus 로고
    • Glycera dibranchiata hemoglobin. X-ray structure of carbon monoxide hemoglobin at 1.5 Å resolution
    • Braden B.C., Arents G., Padlan E.A., and Love W.E. Glycera dibranchiata hemoglobin. X-ray structure of carbon monoxide hemoglobin at 1.5 Å resolution. J. Mol. Biol. 238 (1994) 42-53
    • (1994) J. Mol. Biol. , vol.238 , pp. 42-53
    • Braden, B.C.1    Arents, G.2    Padlan, E.A.3    Love, W.E.4
  • 3
    • 22844452089 scopus 로고    scopus 로고
    • Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin
    • de Sanctis D., et al. Bishistidyl heme hexacoordination, a key structural property in Drosophila melanogaster hemoglobin. J. Biol. Chem. 280 (2005) 27222-27229
    • (2005) J. Biol. Chem. , vol.280 , pp. 27222-27229
    • de Sanctis, D.1
  • 4
    • 33747504697 scopus 로고    scopus 로고
    • Cyanide binding and heme cavity conformational transitions in Drosophila melanogaster hexacoordinate hemoglobin
    • de Sanctis D., et al. Cyanide binding and heme cavity conformational transitions in Drosophila melanogaster hexacoordinate hemoglobin. Biochemistry 45 (2006) 10054-10061
    • (2006) Biochemistry , vol.45 , pp. 10054-10061
    • de Sanctis, D.1
  • 5
    • 0027225143 scopus 로고
    • Polymorphic hemoglobin from a midge larva (Tokunagayusurika akamusi) can be divided into two different types
    • Fukuda M., Takagi T., and Shikama K. Polymorphic hemoglobin from a midge larva (Tokunagayusurika akamusi) can be divided into two different types. Biochim. Biophys. Acta 1157 (1993) 185-191
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 185-191
    • Fukuda, M.1    Takagi, T.2    Shikama, K.3
  • 6
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 7
    • 0017736964 scopus 로고
    • The structure of horse methaemoglobin at 2.0 Å resolution
    • Ladner R.C., Heidner E.J., and Perutz M.F. The structure of horse methaemoglobin at 2.0 Å resolution. J. Mol. Biol. 114 (1977) 385-414
    • (1977) J. Mol. Biol. , vol.114 , pp. 385-414
    • Ladner, R.C.1    Heidner, E.J.2    Perutz, M.F.3
  • 9
    • 0037077231 scopus 로고    scopus 로고
    • Crystal structures of deoxy- and carbonmonoxyhemoglobin F1 from the hagfish Eptatretus burgeri
    • Mito M., et al. Crystal structures of deoxy- and carbonmonoxyhemoglobin F1 from the hagfish Eptatretus burgeri. J. Biol. Chem. 277 (2002) 21898-21905
    • (2002) J. Biol. Chem. , vol.277 , pp. 21898-21905
    • Mito, M.1
  • 10
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris R.J., Perrakis A., and Lamzin V.S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374 (2003) 229-244
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 11
    • 33745571654 scopus 로고    scopus 로고
    • 1.25 Å resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms
    • Park S.Y., Yokoyama T., Shibayama N., Shiro Y., and Tame T.J. 1.25 Å resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. J. Mol. Biol. 360 (2006) 690-701
    • (2006) J. Mol. Biol. , vol.360 , pp. 690-701
    • Park, S.Y.1    Yokoyama, T.2    Shibayama, N.3    Shiro, Y.4    Tame, T.J.5
  • 12
    • 28844471469 scopus 로고    scopus 로고
    • Modulation of oxygen binding to insect hemoglobins: the structure of hemoglobin from the botfly Gasterophilus intestinalis
    • Pesce A., et al. Modulation of oxygen binding to insect hemoglobins: the structure of hemoglobin from the botfly Gasterophilus intestinalis. Protein Sci. 14 (2005) 3057-3063
    • (2005) Protein Sci. , vol.14 , pp. 3057-3063
    • Pesce, A.1
  • 14
    • 0032052760 scopus 로고    scopus 로고
    • Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins
    • Riggs A.F. Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins. J. Exp. Biol. 201 (1998) 1073-1084
    • (1998) J. Exp. Biol. , vol.201 , pp. 1073-1084
    • Riggs, A.F.1
  • 15
    • 0028009317 scopus 로고
    • High-resolution crystallographic analysis of a co-operative dimeric hemoglobin
    • Royer Jr. W.E. High-resolution crystallographic analysis of a co-operative dimeric hemoglobin. J. Mol. Biol. 235 (1994) 657-681
    • (1994) J. Mol. Biol. , vol.235 , pp. 657-681
    • Royer Jr., W.E.1
  • 17
    • 0018800288 scopus 로고
    • Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution
    • Steingemann W., and Weber E. Structure of erythrocruorin in different ligand states refined at 1.4 Å resolution. J. Mol. Biol. 127 (1979) 309-338
    • (1979) J. Mol. Biol. , vol.127 , pp. 309-338
    • Steingemann, W.1    Weber, E.2
  • 18
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 19
    • 0021783302 scopus 로고
    • The structure of invertebrate extracellular hemoglobins (erythrocruorins and chlorocruorins)
    • Vinogradov S.N. The structure of invertebrate extracellular hemoglobins (erythrocruorins and chlorocruorins). Comp. Biochem. Physiol., B 82 (1985) 1-15
    • (1985) Comp. Biochem. Physiol., B , vol.82 , pp. 1-15
    • Vinogradov, S.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.