메뉴 건너뛰기




Volumn 9, Issue 1, 2000, Pages 83-94

Deleterious effects of β-branched residues in the S1 specificity pocket of Streptomyces griseus proteinase B (SGPB): Crystal structures of the turkey ovomucoid third domain variants Ile18I, Val18I, Thr18I, and Ser18I in complex with SGPB

Author keywords

Association equilibrium constants; OMTKY3; Protein inhibitor; Serine proteinase; SGPB; X ray structure; branched amino acids

Indexed keywords

PROTEINASE; SERINE PROTEINASE;

EID: 0033980446     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.1.83     Document Type: Article
Times cited : (20)

References (43)
  • 3
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interactions with proteinases
    • Bode W, Huber R. 1992. Natural protein proteinase inhibitors and their interactions with proteinases. Eur J Biochem 204:433-451.
    • (1992) Eur J Biochem , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (Collaborative Computational Project Number 4). 1994. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr D50:760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 6
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly ML. 1983. Analytical molecular surface calculation. J Appl Crystallogr 15:548-558.
    • (1983) J Appl Crystallogr , vol.15 , pp. 548-558
    • Connolly, M.L.1
  • 7
    • 0015350850 scopus 로고
    • The influence of the geometric properties of the active centre on the specificity of α-chymotrypsin catalysis
    • Dorovska VN, Varfolomeyev SD, Kazanskaya NF, Klyosov AA, Martinek K. 1972. The influence of the geometric properties of the active centre on the specificity of α-chymotrypsin catalysis. FEBS Lett 23:122-124.
    • (1972) FEBS Lett , vol.23 , pp. 122-124
    • Dorovska, V.N.1    Varfolomeyev, S.D.2    Kazanskaya, N.F.3    Klyosov, A.A.4    Martinek, K.5
  • 9
    • 0018780576 scopus 로고
    • Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions
    • Fersht AR, Dingwall C. 1979. Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions. Biochemistry 18:1245-1249.
    • (1979) Biochemistry , vol.18 , pp. 1245-1249
    • Fersht, A.R.1    Dingwall, C.2
  • 10
    • 0027462173 scopus 로고
    • Principles of protein stability derived from protein engineering experiments
    • Fersht AR, Serrano L. 1993. Principles of protein stability derived from protein engineering experiments. Curr Opin Struct Biol 3:75-83.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 75-83
    • Fersht, A.R.1    Serrano, L.2
  • 11
    • 0020172462 scopus 로고
    • Refined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey
    • Fujinaga M, Read RJ, Sielecki AR, Ardelt W, Laskowski M Jr, James MNG. 1982. Refined Crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey. Proc Natl Acad Sci USA 79:4868-4872.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4868-4872
    • Fujinaga, M.1    Read, R.J.2    Sielecki, A.R.3    Ardelt, W.4    Laskowski M., Jr.5    James, M.N.G.6
  • 14
    • 0028856716 scopus 로고
    • Water molecules participate in proteinase-inhibitor interactions: Crystal structures of Leu18, Ala18, Gly18 variants of turkey ovomucoid inhibitor third domain with Streptomyces griseus proteinase B
    • Huang K, Lu W, Anderson S, Laskowski M Jr, James MNG. 1995. Water molecules participate in proteinase-inhibitor interactions: Crystal structures of Leu18, Ala18, Gly18 variants of turkey ovomucoid inhibitor third domain with Streptomyces griseus proteinase B. Protein Sci 4:1985-1997.
    • (1995) Protein Sci , vol.4 , pp. 1985-1997
    • Huang, K.1    Lu, W.2    Anderson, S.3    Laskowski M., Jr.4    James, M.N.G.5
  • 15
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin J, Chothia C. 1990. The structure of protein-protein recognition sites. J Biol Chem 265:16027-16030.
    • (1990) J Biol Chem , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 16
    • 0022333120 scopus 로고
    • Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO
    • Jones TA. 1985. Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. Methods Enzymol 115:157-171.
    • (1985) Methods Enzymol , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard D. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, D.4
  • 19
    • 0024375463 scopus 로고
    • Energetics of complementary side-chain packing in a protein hydrophobic core
    • Kellis JT, Nyberg K, Fersht AR. 1989. Energetics of complementary side-chain packing in a protein hydrophobic core. Biochemistry 28:4914-4922.
    • (1989) Biochemistry , vol.28 , pp. 4914-4922
    • Kellis, J.T.1    Nyberg, K.2    Fersht, A.R.3
  • 20
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt GJ, Jones TA. 1994. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr D50:178-185.
    • (1994) Acta Crystallogr , vol.D50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 21
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M Jr, Kato I. 1980. Protein inhibitors of proteinases. Annu Rev Biochem 49:593-626.
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski M., Jr.1    Kato, I.2
  • 24
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati V. 1952. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallogr 5:802-810.
    • (1952) Acta Crystallogr , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 26
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald ID, Thornton JM. 1994. Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.D.1    Thornton, J.M.2
  • 27
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
    • McGregor MJ, Islam SA, Sternberg MJE. 1987. Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J Mol Biol 198:295-310.
    • (1987) J Mol Biol , vol.198 , pp. 295-310
    • McGregor, M.J.1    Islam, S.A.2    Sternberg, M.J.E.3
  • 28
    • 0002691997 scopus 로고
    • Appendix B: Xtalview users' guide. A software system for protein crystallography
    • McRee DE, ed. San Diego, CA: Academic Press
    • McRee DE. 1993. Appendix B: Xtalview users' guide. A software system for protein crystallography. In: McRee DE, ed. Practical protein crystallography. San Diego, CA: Academic Press. pp 303-374.
    • (1993) Practical Protein Crystallography , pp. 303-374
    • McRee, D.E.1
  • 29
    • 0027932407 scopus 로고
    • C-tail valine is a key residue for stabilization of complex between potato inhibitor and carboxypeptidase A
    • Molina MA, Marino C, Oliva B, Aviles FX, Quero E. 1994. C-tail valine is a key residue for stabilization of complex between potato inhibitor and carboxypeptidase A. J Biol Chem 269(34):21467-21472.
    • (1994) J Biol Chem , vol.269 , Issue.34 , pp. 21467-21472
    • Molina, M.A.1    Marino, C.2    Oliva, B.3    Aviles, F.X.4    Quero, E.5
  • 30
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp K, Honig B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1996. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1996) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 33845280446 scopus 로고
    • Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol and neutral aqueous solution
    • Radzicka A, Wolfenden R. 1988. Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol and neutral aqueous solution. Biochemistry 27:1664-1670.
    • (1988) Biochemistry , vol.27 , pp. 1664-1670
    • Radzicka, A.1    Wolfenden, R.2
  • 34
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read RJ. 1986. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr A42:140-149.
    • (1986) Acta Crystallogr , vol.A42 , pp. 140-149
    • Read, R.J.1
  • 35
    • 0021102433 scopus 로고
    • Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8 Å resolution
    • Read RJ, Fujinaga M, Sielecki AR, James MNG. 1983. Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8 Å resolution. Biochemistry 22:4420-4433.
    • (1983) Biochemistry , vol.22 , pp. 4420-4433
    • Read, R.J.1    Fujinaga, M.2    Sielecki, A.R.3    James, M.N.G.4
  • 36
    • 0003150431 scopus 로고
    • Introduction to the protein inhibitors: X-ray crystallography
    • Barrett AJ, Salvesen G, eds. Amsterdam: Elsevier Science Publishers B.V.
    • Read RJ, James MNG. 1986. Introduction to the protein inhibitors: X-ray crystallography. In: Barrett AJ, Salvesen G, eds. Proteinase inhibitors. Amsterdam: Elsevier Science Publishers B.V. pp 301-336.
    • (1986) Proteinase Inhibitors , pp. 301-336
    • Read, R.J.1    James, M.N.G.2
  • 37
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model software evaluation: Three related resources
    • Rodriguez R, Chinea G, Lopez N, Pons T, Vriend G. 1998. Homology modeling, model software evaluation: Three related resources. Bioinformatics 14:523-528.
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 38
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, Berger A. 1967. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27:157-162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 39
    • 0027208112 scopus 로고
    • Rotamers: To be or not to be? An analysis of amino acid side-chain conformations in globular proteins
    • Schrauber H, Eisenhaber F, Argos P. 1993. Rotamers: To be or not to be? An analysis of amino acid side-chain conformations in globular proteins. J Mol Biol 230:592-612.
    • (1993) J Mol Biol , vol.230 , pp. 592-612
    • Schrauber, H.1    Eisenhaber, F.2    Argos, P.3
  • 40
    • 0031587287 scopus 로고    scopus 로고
    • Free energies of amino acid side-chain rotamers in α-helices, β-sheets and α-helix N-caps
    • Stapley BJ, Doig AJ. 1997. Free energies of amino acid side-chain rotamers in α-helices, β-sheets and α-helix N-caps. J Mol Biol 272:456-464.
    • (1997) J Mol Biol , vol.272 , pp. 456-464
    • Stapley, B.J.1    Doig, A.J.2
  • 42
    • 0029147823 scopus 로고
    • Intrinsic φ, ψ propensities of amino acids, derived from the coil regions of known structures
    • Swindells MB, MacArthur MW, Thornton JM. 1995. Intrinsic φ, ψ propensities of amino acids, derived from the coil regions of known structures. Nature Struct Biol 2:596-603.
    • (1995) Nature Struct Biol , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 43
    • 84945074880 scopus 로고
    • Conjugate-direction minimization: An improved method for the refinement of macromolecules
    • Tronrud DE. 1992. Conjugate-direction minimization: An improved method for the refinement of macromolecules. Acta Crystallogr A48:912-916.
    • (1992) Acta Crystallogr , vol.A48 , pp. 912-916
    • Tronrud, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.