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Volumn 30, Issue 1, 1998, Pages 34-42

Conserved water molecules in the specificity pocket of serine proteases and the molecular mechanism of Na+ binding

Author keywords

Allostery; Buried water molecules; Molecular recognition; Na+ site; Thrombin; Trypsin

Indexed keywords

AQUAPORIN; PLASMIN; PROTEINASE; SERINE PROTEINASE; SODIUM; TISSUE PLASMINOGEN ACTIVATOR; TRYPSIN; UROKINASE; WATER;

EID: 0031974656     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980101)30:1<34::AID-PROT3>3.0.CO;2-K     Document Type: Article
Times cited : (46)

References (22)
  • 1
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings, R.D., Barrett, A.J. Evolutionary families of peptidases. Biochem. J. 290:205-218, 1993.
    • (1993) Biochem. J. , vol.290 , pp. 205-218
    • Rawlings, R.D.1    Barrett, A.J.2
  • 2
    • 0029962944 scopus 로고    scopus 로고
    • Conservation and variability in the structures of serine proteinases of the chymotrypsin family
    • Lesk, A.M., Fordham, W.D. Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J. Mol. Biol. 258:501-537, 1996.
    • (1996) J. Mol. Biol. , vol.258 , pp. 501-537
    • Lesk, A.M.1    Fordham, W.D.2
  • 3
    • 0023512935 scopus 로고
    • Reconstructing the evolution of vertebrate blood coagulation from a consideration of the amino acid sequences of clotting factors
    • Doolittle, R.F., Feng, D.F. Reconstructing the evolution of vertebrate blood coagulation from a consideration of the amino acid sequences of clotting factors. Cold Spring Harbor Symp. Quant. Biol. 52:869-874, 1987.
    • (1987) Cold Spring Harbor Symp. Quant. Biol. , vol.52 , pp. 869-874
    • Doolittle, R.F.1    Feng, D.F.2
  • 4
    • 0029785840 scopus 로고    scopus 로고
    • +-induced allosteric regulation of catalytic activity in serine proteases
    • +-induced allosteric regulation of catalytic activity in serine proteases. Proc. Natl. Acad. Sci. U.S.A. 93:10653-10656, 1996.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10653-10656
    • Dang, Q.D.1    Di Cera, E.2
  • 8
    • 0024791521 scopus 로고
    • Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density
    • Bartunik, H.D., Summers, L.J., Bartsch, H.H. Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density. J. Mol. Biol. 210:813-828, 1989.
    • (1989) J. Mol. Biol. , vol.210 , pp. 813-828
    • Bartunik, H.D.1    Summers, L.J.2    Bartsch, H.H.3
  • 9
    • 0027068111 scopus 로고
    • Buried water in homologous serine proteases
    • Sreenivasan, U., Axelsen, P.H. Buried water in homologous serine proteases. Biochemistry 31:12785-12791, 1992.
    • (1992) Biochemistry , vol.31 , pp. 12785-12791
    • Sreenivasan, U.1    Axelsen, P.H.2
  • 10
    • 0026547998 scopus 로고
    • Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction
    • Finer-Moore, J.S., Kossiakoff, A.A., Hurley, J.H., Earnest, T., Stroud, R.M. Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction. Proteins 12:203-222, 1992.
    • (1992) Proteins , vol.12 , pp. 203-222
    • Finer-Moore, J.S.1    Kossiakoff, A.A.2    Hurley, J.H.3    Earnest, T.4    Stroud, R.M.5
  • 11
    • 0028586082 scopus 로고
    • The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: Changes accompanying activation and exosite binding to thrombin
    • Vijayalakshmi, J., Padmanabhan, K.P., Mann, K.G., Tulinsky, A. The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: changes accompanying activation and exosite binding to thrombin. Protein Sci. 3:2254-2271, 1994.
    • (1994) Protein Sci. , vol.3 , pp. 2254-2271
    • Vijayalakshmi, J.1    Padmanabhan, K.P.2    Mann, K.G.3    Tulinsky, A.4
  • 13
    • 0025756173 scopus 로고
    • Structure of β-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that β-chymotrypsin is a covalent acyl-enzyme adduct at low pH
    • Dixon, M.M., Brennan, R.G., Matthews, B.W. Structure of β-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that β-chymotrypsin is a covalent acyl-enzyme adduct at low pH. Int. J. Biol. Macromol. 13:89-96, 1991.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 89-96
    • Dixon, M.M.1    Brennan, R.G.2    Matthews, B.W.3
  • 15
    • 0022801412 scopus 로고
    • X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor
    • Bode, W., Wei, A.Z., Huber, R., Meyer, E., Travis, J., Neumann, S. X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor. EMBO J. 5:2453-2458, 1986.
    • (1986) EMBO J. , vol.5 , pp. 2453-2458
    • Bode, W.1    Wei, A.Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 16
    • 0023192209 scopus 로고
    • Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 Å resolution
    • Fujinaga, M., James, M.N.G. Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 Å resolution. J. Mol. Biol. 195:373-396, 1987.
    • (1987) J. Mol. Biol. , vol.195 , pp. 373-396
    • Fujinaga, M.1    James, M.N.G.2
  • 17
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of mammalian serine proteases
    • Greer, J. Comparative modeling methods: application to the family of mammalian serine proteases. Proteins 7:317-334, 1990.
    • (1990) Proteins , vol.7 , pp. 317-334
    • Greer, J.1
  • 19
    • 0030036162 scopus 로고    scopus 로고
    • Large heat capacity change in a protein-monovalent cation interaction
    • Guinto, E.R., Di Cera, E. Large heat capacity change in a protein-monovalent cation interaction. Biochemistry 35: 8800-8804, 1996.
    • (1996) Biochemistry , vol.35 , pp. 8800-8804
    • Guinto, E.R.1    Di Cera, E.2
  • 21
    • 0029992043 scopus 로고    scopus 로고
    • Release of fibrinopeptides by the slow and fast forms of thrombin
    • Vindigni, A., Di Cera, E. Release of fibrinopeptides by the slow and fast forms of thrombin. Biochemistry 35:4417-4426, 1996.
    • (1996) Biochemistry , vol.35 , pp. 4417-4426
    • Vindigni, A.1    Di Cera, E.2
  • 22
    • 0031052393 scopus 로고    scopus 로고
    • Rational engineering of catalytic activity and specificity in a serine protease
    • Dang, Q.D., Guinto, E.R., Di Cera, E. Rational engineering of catalytic activity and specificity in a serine protease. Nature Biotechnol. 15:146-149, 1997.
    • (1997) Nature Biotechnol. , vol.15 , pp. 146-149
    • Dang, Q.D.1    Guinto, E.R.2    Di Cera, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.