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Volumn 113, Issue 24, 1991, Pages 9382-9384

X-ray Crystal Structure of the HIV Protease Complex with L-700,417, an Inhibitor with Pseudo C2 Symmetry

Author keywords

[No Author keywords available]

Indexed keywords

2,6 DIBENZYL 4 HYDROXY N,N' BIS(2 HYDROXY 1 INDANYL) 1,7 HEPTANEDIAMIDE; ENZYME INHIBITOR; L 700417; PROTEINASE; UNCLASSIFIED DRUG;

EID: 0026350729     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja00024a061     Document Type: Article
Times cited : (149)

References (32)
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    • Jacks, T. Nature 1988, 331, 280–283.
    • (1988) Nature , vol.331 , pp. 280-283
    • Jacks, T.1
  • 16
    • 85023280797 scopus 로고    scopus 로고
    • N, N′-Bis(2(R)-hydroxy-l(S)-indanyl)-2(R),6(R)-bis(phenyl-methyl)-4-hydroxy-1,7-heptanediamide.
    • N, N′-Bis(2(R)-hydroxy-l(S)-indanyl)-2(R),6(R)-bis(phenyl-methyl)-4-hydroxy-1,7-heptanediamide. Vacca, J.; Askin, D., manuscript in preparation.
    • manuscript in preparation.
    • Vacca, J.1    Askin, D.2
  • 19
    • 84967851020 scopus 로고
    • The HI VP complex with 2 was cocrystallized (enzyme and inhibitor in a 1:2 ratio) from NaCl by vapor diffusion as described previously for the HIVP—APS complex, and the crystals were isomorphous with the ortho-rhombic HIVP—APS crystals (P21212, a = 58.88 Å, b = 86.80 Å, c = 46.79 Å).11 Data were collected from a single crystal of enzyme-inhibitor complex using Cu Kα X-rays (λ = 1.5418) and a Siemens multiwire X-ray area detector equipped with a graphite monochromator and processed using the Xengen software
    • The HI VP complex with 2 was cocrystallized (enzyme and inhibitor in a 1:2 ratio) from NaCl by vapor diffusion as described previously for the HIVP—APS complex, and the crystals were isomorphous with the ortho-rhombic HIVP—APS crystals (P21212, a = 58.88 Å, b = 86.80 Å, c = 46.79 Å).11 Data were collected from a single crystal of enzyme-inhibitor complex using Cu Kα X-rays (λ = 1.5418) and a Siemens multiwire X-ray area detector equipped with a graphite monochromator and processed using the Xengen software (Howard, A. J.; Gilliland, G. L.; Finzel, B. C.; Poulos, T. L.; Ohlendorf, D. H.; Selemme, F. R. J. Appl. Crystallogr. 1987, 20, 383–387).
    • (1987) J. Appl. Crystallogr. , vol.20 , pp. 383-387
    • Howard, A.J.1    Gilliland, G.L.2    Finzel, B.C.3    Poulos, T.L.4    Ohlendorf, D.H.5    Selemme, F.R.6
  • 20
    • 0022333121 scopus 로고
    • The data extended to 2.1-Å resolution, was 97.2% complete, had 70% of the intensities observed greater than 2σ(I), and had an overall Rmerge equal to 0.07. All measured reflections were used in refinement
    • The data extended to 2.1-Å resolution, was 97.2% complete, had 70% of the intensities observed greater than 2σ(I), and had an overall Rmerge equal to 0.07. All measured reflections were used in refinement (Hendrickson, W. A. Methods Enzymol. 1985, 115, 252–270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 28
  • 29
    • 0017429069 scopus 로고
    • Using an upper estimate for the energetic gian of removing hydrophobic surfaces from solvent of 25 cal/Å2
    • Using an upper estimate for the energetic gian of removing hydrophobic surfaces from solvent of 25 cal/Å2 Richards, F. M. Annu. Rev. Biophys. Bioeng. 1977, 6, 151–176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 30
    • 0016606973 scopus 로고
    • Clearly hydrophobic interactions must be offset by unfavorable consequences of binding such as the entropic cost of freezing the inhibitor conformation.
    • Chothia, C. Nature (London) 1975, 254, 304–308. Clearly hydrophobic interactions must be offset by unfavorable consequences of binding such as the entropic cost of freezing the inhibitor conformation.
    • (1975) Nature (London) , vol.254 , pp. 304-308
    • Chothia, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.