메뉴 건너뛰기




Volumn 389, Issue 2, 2005, Pages 365-371

Observation of a tetrahedral reaction intermediate in the HIV-1 protease-substrate complex

Author keywords

Catalysis; HIV 1 protease; Inhibitor; Reaction intermediate; Transition state; X ray crystallography

Indexed keywords

CATALYSIS; COMPLEXATION; CRYSTAL STRUCTURE; DRUG DOSAGE; ENZYME INHIBITION; HYDROGEN BONDS; REACTION KINETICS; SUBSTRATES; X RAY ANALYSIS;

EID: 22544467240     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041804     Document Type: Article
Times cited : (29)

References (22)
  • 2
    • 0142186280 scopus 로고    scopus 로고
    • Determinants of survival following HIV-1 seroconversion after the introduction of HAART
    • Porter, K., Babiker, A., Bhaskaran, K., Darbyshire, J., Pezzotti, P., Porter, K. and Walker, A. S. (CASCADE Collaboration) (2003) Determinants of survival following HIV-1 seroconversion after the introduction of HAART. Lancet 362, 1267-1274
    • (2003) Lancet , vol.362 , pp. 1267-1274
    • Porter, K.1    Babiker, A.2    Bhaskaran, K.3    Darbyshire, J.4    Pezzotti, P.5    Porter, K.6    Walker, A.S.7
  • 4
    • 0037471276 scopus 로고    scopus 로고
    • Viral breakthrough after suppression with highly active antiretroviral therapy: Experience from 233 individuals with viral loads of less than 50 copies/ml followed for up to 4 years
    • Lampe, F. C., Johnson, M. A., Lipman, M., Loveday, C., Youle, M., Ransom, D., Sabin, C. A., Tyrer, M. and Phillips, A. N. (2003) Viral breakthrough after suppression with highly active antiretroviral therapy: experience from 233 individuals with viral loads of less than 50 copies/ml followed for up to 4 years. AIDS 17, 759-777
    • (2003) AIDS , vol.17 , pp. 759-777
    • Lampe, F.C.1    Johnson, M.A.2    Lipman, M.3    Loveday, C.4    Youle, M.5    Ransom, D.6    Sabin, C.A.7    Tyrer, M.8    Phillips, A.N.9
  • 5
    • 0031804609 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 protease: A major success of structure-assisted drug design
    • Wlodawer, A. and Vondrasek, J. (1998) Inhibitors of HIV-1 protease: a major success of structure-assisted drug design. Annu. Rev. Biophys. Biomol. Struct. 27, 249-284
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 249-284
    • Wlodawer, A.1    Vondrasek, J.2
  • 6
    • 0029814481 scopus 로고    scopus 로고
    • Three-dimensional structures of HIV-1 and SIV protease product complexes
    • Rose, R. B., Craik, C. S., Douglas, N. L. and Stroud, R. M. (1996) Three-dimensional structures of HIV-1 and SIV protease product complexes. Biochemistry 35, 12933-12944
    • (1996) Biochemistry , vol.35 , pp. 12933-12944
    • Rose, R.B.1    Craik, C.S.2    Douglas, N.L.3    Stroud, R.M.4
  • 7
    • 0036121219 scopus 로고    scopus 로고
    • Substrate shape determines specificity of recognition for HIV-1 protease: Analysis of crystal structures of six substrate complexes
    • Jeyabalan, M. P., Nalivaika, E. and Schiffer, C. A. (2002) Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. Structure 10, 369-381
    • (2002) Structure , vol.10 , pp. 369-381
    • Jeyabalan, M.P.1    Nalivaika, E.2    Schiffer, C.A.3
  • 8
    • 1642534610 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation
    • Aertgeerts, K., Ye, S., Tennant, M. G., Kraus, M. L., Rogers, J., Sang, B. C., Skene, R. J., Webb, D. R. and Prasad, G. S. (2004) Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Sci. 13, 412-421
    • (2004) Protein Sci. , vol.13 , pp. 412-421
    • Aertgeerts, K.1    Ye, S.2    Tennant, M.G.3    Kraus, M.L.4    Rogers, J.5    Sang, B.C.6    Skene, R.J.7    Webb, D.R.8    Prasad, G.S.9
  • 9
    • 0042131827 scopus 로고    scopus 로고
    • Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
    • Thoma, R., Loffler, B., Stihle, M., Huber, W., Ruf, A. and Hennig, M. (2003) Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure 11, 947-959
    • (2003) Structure , vol.11 , pp. 947-959
    • Thoma, R.1    Loffler, B.2    Stihle, M.3    Huber, W.4    Ruf, A.5    Hennig, M.6
  • 12
    • 0025641617 scopus 로고
    • Stability and activity of human immunodeficiency virus protease: Comparison of a natural dimer with a homologous single chain tethered dimer
    • Cheng, Y.-S. E., Yin, F. H., Foundling, S., Blomstrom, D. and Kettner, C. A. (1990) Stability and activity of human immunodeficiency virus protease: comparison of a natural dimer with a homologous single chain tethered dimer. Proc. Natl. Acad. Sci. U.S.A. 87, 9660-9664
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9660-9664
    • Cheng, Y.-S.E.1    Yin, F.H.2    Foundling, S.3    Blomstrom, D.4    Kettner, C.A.5
  • 14
    • 0037350008 scopus 로고    scopus 로고
    • Adaptability and flexibility of HIV-1 protease
    • Kumar, M. and Hosur, M. V. (2003) Adaptability and flexibility of HIV-1 protease. Eur. J. Biochem. 270, 1231-1239
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1231-1239
    • Kumar, M.1    Hosur, M.V.2
  • 15
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • (Swyer, L., Isaacs, N. and Baily, S., eds.), SERC Daresbury Laboratory, Warrington, U.K.
    • Otwinowski, Z. (1993) Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing (Swyer, L., Isaacs, N. and Baily, S., eds.), pp. 56-62, SERC Daresbury Laboratory, Warrington, U.K.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0035314020 scopus 로고    scopus 로고
    • 1.9 Å X-ray study shows closed flap conformation in crystals of tethered HIV-1 PR
    • Pillai, B., Kannan, K. K. and Hosur, M. V. (2001) 1.9 Å X-ray study shows closed flap conformation in crystals of tethered HIV-1 PR. Proteins 43, 57-64
    • (2001) Proteins , vol.43 , pp. 57-64
    • Pillai, B.1    Kannan, K.K.2    Hosur, M.V.3
  • 20
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn, B. M. (2002) Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem. Rev. 102, 4431-4458
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 21
    • 0033136041 scopus 로고    scopus 로고
    • Conformational aspects of inhibitor design: Enzyme-substrate interactions in the transition state
    • Wolfenden, R. (1999) Conformational aspects of inhibitor design: enzyme-substrate interactions in the transition state. Bioorg. Med. Chem. 7, 647-652
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 647-652
    • Wolfenden, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.