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Volumn 121, Issue 2, 1999, Pages 478-479

Caged HIV-1 protease: Dimerization is independent of the ionization state of the active site aspartates

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; PROTEINASE;

EID: 0033585614     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9838054     Document Type: Article
Times cited : (31)

References (45)
  • 3
    • 0030849517 scopus 로고    scopus 로고
    • For a review on HIV-1 protease inhibitors currently used for the treatment of AIDS, see: Vacca, J. P. Drug Discovery Today 1997, 7, 261.
    • (1997) Drug Discovery Today , vol.7 , pp. 261
    • Vacca, J.P.1
  • 12
    • 84920310143 scopus 로고    scopus 로고
    • note
    • 8 have demonstrated that a mutant protease containing Asn25 could form a dimer, albeit of lesser stability.
  • 36
    • 84920310142 scopus 로고    scopus 로고
    • note
    • 8 All constructs encoded a hexahistidine fusion peptide.
  • 37
    • 84920310141 scopus 로고    scopus 로고
    • note
    • Restoration of proteolytic activity was possible after purification of the monomer by nickel affinity chromatography, followed by dialysis.
  • 39
    • 0024406911 scopus 로고
    • 8b (a) Loeb, D. D.; Swanstrom, R.; Everitt, L.; Manchester, M.; Stamper, S. E.; Hutchison, C. A., III Nature 1989, 340, 397. (b) Krausslich, H.-G. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 3213. The minimal (13%) activity measured for the dimeric protease containing 5 at position 25 is attributed to adventitious solvolysis during protein sample preparation.
    • (1989) Nature , vol.340 , pp. 397
    • Loeb, D.D.1    Swanstrom, R.2    Everitt, L.3    Manchester, M.4    Stamper, S.E.5    Hutchison C.A. III6
  • 40
    • 0026322839 scopus 로고
    • 8b (a) Loeb, D. D.; Swanstrom, R.; Everitt, L.; Manchester, M.; Stamper, S. E.; Hutchison, C. A., III Nature 1989, 340, 397. (b) Krausslich, H.-G. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 3213. The minimal (13%) activity measured for the dimeric protease containing 5 at position 25 is attributed to adventitious solvolysis during protein sample preparation.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3213
    • Krausslich, H.-G.1
  • 42
    • 84920310140 scopus 로고    scopus 로고
    • note
    • Under denaturing conditions, in the presence of 6 M urea and 2 mM catalyst, Pd-catalyzed deblocking afforded an active protease monomer having a specific activity 85% that of wild type (16 h incubation. 23°C). whereas the caged enzyme was inactive (Supporting Information. Figure 3).
  • 43
    • 0032541289 scopus 로고    scopus 로고
    • It may be possible to employ this protecting group under native conditions using wcll-solvated aspartates on the surface of enzymes. See: Pollit, S. K.; Schultz, P. G. Angew. Chem., Int. Ed. Engl. 1998, 37, 2104.
    • (1998) Angew. Chem., Int. Ed. Engl. , vol.37 , pp. 2104
    • Pollit, S.K.1    Schultz, P.G.2
  • 44
    • 84920310139 scopus 로고    scopus 로고
    • note
    • That the formed dimer had a structure fundamentally analogous to that of the native enzyme can be appreciated by the full restoration of enzymic activity following irradiation of the caged dimer (Figure 2).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.