메뉴 건너뛰기




Volumn 1724, Issue 3, 2005, Pages 385-393

Internal cavities and ligand passageways in human hemoglobin characterized by molecular dynamics simulations

Author keywords

Cytoglobin; Group I truncated hemoglobins; Human hemoglobin; Internal cavities; Ligand migration; Molecular dynamics; Myoglobin; Xenon docking sites

Indexed keywords

HEME; HEMOGLOBIN; MYOGLOBIN; PROTEIN SUBUNIT; WATER; XENON;

EID: 23144439273     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2005.05.014     Document Type: Review
Times cited : (25)

References (32)
  • 1
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 angstroms
    • R.F. Tilton, I.D. Kuntz, and G.A. Petsko Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 angstroms Biochemistry 23 1984 2849 2857
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton, R.F.1    Kuntz, I.D.2    Petsko, G.A.3
  • 2
    • 0034867130 scopus 로고    scopus 로고
    • Cavities and packing defects in the structural dynamics of myoglobin
    • M. Brunori, and Q.H. Gibson Cavities and packing defects in the structural dynamics of myoglobin EMBO Rep. 2 2001 674 679
    • (2001) EMBO Rep. , vol.2 , pp. 674-679
    • Brunori, M.1    Gibson, Q.H.2
  • 5
    • 0025600834 scopus 로고
    • Enhanced sampling in molecular dynamics: Use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin
    • R. Elber, and M. Karplus Enhanced sampling in molecular dynamics: use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin J. Am. Chem. Soc. 112 1990 9161 9175
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9161-9175
    • Elber, R.1    Karplus, M.2
  • 6
    • 0030031593 scopus 로고    scopus 로고
    • Distal cavity fluctuations in myoglobin: Protein motion and ligand diffusion
    • M.L. Carlson, R.M. Regan, and Q.H. Gibson Distal cavity fluctuations in myoglobin: protein motion and ligand diffusion Biochemistry 35 1996 1125 1136
    • (1996) Biochemistry , vol.35 , pp. 1125-1136
    • Carlson, M.L.1    Regan, R.M.2    Gibson, Q.H.3
  • 7
    • 0030821996 scopus 로고    scopus 로고
    • Initial trajectory of carbon monoxide after photodissociation from myoglobin at cryogenic temperatures
    • T. Teng, V. Srajer, and K. Moffat Initial trajectory of carbon monoxide after photodissociation from myoglobin at cryogenic temperatures Biochemistry 36 1997 12087 12100
    • (1997) Biochemistry , vol.36 , pp. 12087-12100
    • Teng, T.1    Srajer, V.2    Moffat, K.3
  • 8
    • 0031880931 scopus 로고    scopus 로고
    • Computer simulations of carbon monoxide photodissociation in myoglobin: Structural interpretation of the B states
    • J. Meller, and R. Elber Computer simulations of carbon monoxide photodissociation in myoglobin: structural interpretation of the B states Biophys. J. 74 1998 789 802
    • (1998) Biophys. J. , vol.74 , pp. 789-802
    • Meller, J.1    Elber, R.2
  • 9
    • 0034519834 scopus 로고    scopus 로고
    • Trapping intermediates in the crystal: Ligand binding to myoglobin
    • I. Schlichting, and K. Chu Trapping intermediates in the crystal: ligand binding to myoglobin Curr. Opin. Struck. Biol. 10 2000 744 752
    • (2000) Curr. Opin. Struck. Biol. , vol.10 , pp. 744-752
    • Schlichting, I.1    Chu, K.2
  • 11
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction
    • V. Srajer, Z. Ren, T. Teng, M. Schmidt, T. Ursby, D. Bourgeois, C. Pradervand, W. Schildkamp, M. Wulff, and K. Moffat Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction Biochemistry 40 2001 13802 13815
    • (2001) Biochemistry , vol.40 , pp. 13802-13815
    • Srajer, V.1    Ren, Z.2    Teng, T.3    Schmidt, M.4    Ursby, T.5    Bourgeois, D.6    Pradervand, C.7    Schildkamp, W.8    Wulff, M.9    Moffat, K.10
  • 13
    • 2942655520 scopus 로고    scopus 로고
    • Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin
    • C. Bossa, M. Anselmi, D. Roccatano, A. Amadei, B. Vallone, M. Brunori, and A. Di Nola Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin Biophys. J. 86 2004 3855 3862
    • (2004) Biophys. J. , vol.86 , pp. 3855-3862
    • Bossa, C.1    Anselmi, M.2    Roccatano, D.3    Amadei, A.4    Vallone, B.5    Brunori, M.6    Di Nola, A.7
  • 14
    • 0346057931 scopus 로고    scopus 로고
    • Competition with Xenon elicits ligand migration and escape pathways in myoglobin
    • C. Tetreau, Y. Blouquit, E. Novikov, E. Quiniou, and D. Lavalette Competition with Xenon elicits ligand migration and escape pathways in myoglobin Biophys. J. 86 2004 435 447
    • (2004) Biophys. J. , vol.86 , pp. 435-447
    • Tetreau, C.1    Blouquit, Y.2    Novikov, E.3    Quiniou, E.4    Lavalette, D.5
  • 15
    • 1842815139 scopus 로고    scopus 로고
    • Kinetic proofreading by the cavity system of myoglobin: Protection from poisoning
    • W. Radding, and G.N. Phillips Jr. Kinetic proofreading by the cavity system of myoglobin: protection from poisoning BioEssays 26 2004 422 433
    • (2004) BioEssays , vol.26 , pp. 422-433
    • Radding, W.1    Phillips Jr., G.N.2
  • 19
    • 0036099514 scopus 로고    scopus 로고
    • New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations
    • L. Mouawad, D. Perahia, C.H. Robert, and C. Guilbert New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations Biophys. J. 82 2002 3224 3245
    • (2002) Biophys. J. , vol.82 , pp. 3224-3245
    • Mouawad, L.1    Perahia, D.2    Robert, C.H.3    Guilbert, C.4
  • 20
    • 0029633176 scopus 로고
    • A method to explore transition paths in macromolecules. Applications to hemoglobin and phosphoglycerate kinase
    • C. Guilbert, D. Perahia, and L. Mouawad A method to explore transition paths in macromolecules. Applications to hemoglobin and phosphoglycerate kinase Comp. Phys. Comm. 91 1995 263 273
    • (1995) Comp. Phys. Comm. , vol.91 , pp. 263-273
    • Guilbert, C.1    Perahia, D.2    Mouawad, L.3
  • 22
    • 0032190305 scopus 로고    scopus 로고
    • Analytical shape computation of macromolecules: I. Molecular area and volume through alpha shape
    • J. Liang, H. Edelsbrunner, P. Fu, P.V. Sudhakar, and S. Subramaniam Analytical shape computation of macromolecules: I. Molecular area and volume through alpha shape Proteins 33 1998 1 17
    • (1998) Proteins , vol.33 , pp. 1-17
    • Liang, J.1    Edelsbrunner, H.2    Fu, P.3    Sudhakar, P.V.4    Subramaniam, S.5
  • 24
    • 33544456104 scopus 로고    scopus 로고
    • E.C. Liong, Rice University, Houston, TX 1999.
    • E.C. Liong, Rice University, Houston, TX 1999.
  • 25
    • 0034624691 scopus 로고    scopus 로고
    • Ligand binding and conformational motion in myoglobin
    • A. Ostermann, R. Waschipky, F.G. Parak, and G.U. Nienhaus Ligand binding and conformational motion in myoglobin Nature 404 2000 205 208
    • (2000) Nature , vol.404 , pp. 205-208
    • Ostermann, A.1    Waschipky, R.2    Parak, F.G.3    Nienhaus, G.U.4
  • 29
    • 0021683974 scopus 로고
    • The crystal structure of human deoxyhaemoglobin at 1.74 angstroms resolution
    • G. Fermi, M.F. Perutz, B. Shaanan, and R. Fourme The crystal structure of human deoxyhaemoglobin at 1.74 angstroms 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
  • 30
    • 0024562782 scopus 로고
    • Myoglobin and haemoglobin: Role of distal residues in reactions with haem ligands
    • M.F. Perutz Myoglobin and haemoglobin: role of distal residues in reactions with haem ligands Trends Biochem. Sci. 14 1989 42 44
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 42-44
    • Perutz, M.F.1
  • 32
    • 0025785220 scopus 로고
    • Migration of small molecules through the structure of hemoglobin: Evidence for gating in a protein electron-transfert reaction
    • J. Feitelson, and G. McLendon Migration of small molecules through the structure of hemoglobin: evidence for gating in a protein electron-transfert reaction Biochemistry 30 1991 5051 5055
    • (1991) Biochemistry , vol.30 , pp. 5051-5055
    • Feitelson, J.1    McLendon, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.