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Volumn 34, Issue 1, 2009, Pages 27-34

Conserved water-mediated H-bonding dynamics of catalytic Asn 175 in plant thiol protease

Author keywords

Conserved water in molecular recognition; MD simulation; Plant cysteine protease

Indexed keywords

ASPARAGINE; THIOL PROTEINASE; WATER;

EID: 67649868605     PISSN: 02505991     EISSN: 02505991     Source Type: Journal    
DOI: 10.1007/s12038-009-0006-6     Document Type: Article
Times cited : (9)

References (24)
  • 1
    • 33745132659 scopus 로고    scopus 로고
    • High-resolution complex of papain with remnants of a cysteine protease inhibitor derived from Trypanosoma brucei
    • M. S. Alphey W. N. Hunter 2006 High-resolution complex of papain with remnants of a cysteine protease inhibitor derived from Trypanosoma brucei Acta Crystalogr. F62 504 508
    • (2006) Acta Crystalogr. , vol.62 , pp. 504-508
    • Alphey, M.S.1    Hunter, W.N.2
  • 2
    • 0001452325 scopus 로고
    • Crystallographic refinement of the structure of actinidin at 1.7 Å resolution by Fast Fourier Least-Squares Methods
    • E. N. Baker E. J. Dodson 1980 Crystallographic refinement of the structure of actinidin at 1.7 Å resolution by Fast Fourier Least-Squares Methods Acta Crystalogr. A36 559 572
    • (1980) Acta Crystalogr. , vol.36 , pp. 559-572
    • Baker, E.N.1    Dodson, E.J.2
  • 5
    • 11144230087 scopus 로고    scopus 로고
    • A novel method reveals that solvent water favors polyproline II over β-strand conformation in peptide and unfolded proteins: conditional hydrophobic accessible surface area (CHASA)
    • P. J. Fleming N. C. Fitzkee M. Mezei R. Srinivasan G. D. Rose 2005 A novel method reveals that solvent water favors polyproline II over β-strand conformation in peptide and unfolded proteins: conditional hydrophobic accessible surface area (CHASA) Protein Sci. 14 111 118
    • (2005) Protein Sci. , vol.14 , pp. 111-118
    • Fleming, P.J.1    Fitzkee, N.C.2    Mezei, M.3    Srinivasan, R.4    Rose, G.D.5
  • 8
    • 4744365526 scopus 로고    scopus 로고
    • Two polymorphs of a covalent complex between papain and a diazomethylketone inhibitor
    • R. Janowski M. Kozak E. Jankowska Z. Grzonka M. Jaskolski 2004 Two polymorphs of a covalent complex between papain and a diazomethylketone inhibitor J. Pept. Res. 64 141 150
    • (2004) J. Pept. Res. , vol.64 , pp. 141-150
    • Janowski, R.1    Kozak, M.2    Jankowska, E.3    Grzonka, Z.4    Jaskolski, M.5
  • 12
    • 0022475935 scopus 로고
    • Elevations of cathepsin B and cathepsin L activities in forelimb and hind muscles of genetically dystrophic mice
    • K. Komatsu K. Tsukuda J. Hosoya S. Satoh 1986 Elevations of cathepsin B and cathepsin L activities in forelimb and hind muscles of genetically dystrophic mice Exp. Neurol. 93 642 646
    • (1986) Exp. Neurol. , vol.93 , pp. 642-646
    • Komatsu, K.1    Tsukuda, K.2    Hosoya, J.3    Satoh, S.4
  • 14
    • 2942641889 scopus 로고    scopus 로고
    • Cluster analysis of water molecules in alanine racemase and their putative structural role
    • G. Mustata J. M. Briggs 2004 Cluster analysis of water molecules in alanine racemase and their putative structural role Protein Eng. Des. Sel. 17 223 234
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 223-234
    • Mustata, G.1    Briggs, J.M.2
  • 16
    • 33846493571 scopus 로고    scopus 로고
    • Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure
    • P. A. O'Farrell L. Joshua-Tor 2007 Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure Biochem. J. 401 421 428
    • (2007) Biochem. J. , vol.401 , pp. 421-428
    • O'Farrell, P.A.1    Joshua-Tor, L.2
  • 17
    • 0003035460 scopus 로고
    • Structure of monoclinic papain at 1.60 Angstrom resolution
    • R. W. Pickersgill G. W. Harris E. Garman 1992 Structure of monoclinic papain at 1.60 Angstrom resolution Acta Crystalogr. B48 59 67
    • (1992) Acta Crystalogr. , vol.48 , pp. 59-67
    • Pickersgill, R.W.1    Harris, G.W.2    Garman, E.3
  • 20
    • 0016115206 scopus 로고
    • Mercaptide-imidazolium ion-pair: the reactive nucleophile in papain catalysis
    • L. Polgár 1974 Mercaptide-imidazolium ion-pair: the reactive nucleophile in papain catalysis FEBS Lett. 47 15 18
    • (1974) FEBS Lett. , vol.47 , pp. 15-18
    • Polgár, L.1
  • 21
    • 0026556022 scopus 로고
    • On the interpretation of biochemical data by molecular dynamics computer simulation
    • W. F. Van Gunsteren A. E. Mark 1992 On the interpretation of biochemical data by molecular dynamics computer simulation Eur. J. Biochem. 204 947 961
    • (1992) Eur. J. Biochem. , vol.204 , pp. 947-961
    • Van Gunsteren, W.F.1    Mark, A.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.