Unexpected binding mode of a cyclic sulfamide HIV-1 protease inhibitor

被引：132

作者：

Backbro, K

Lowgren, S

Osterlund, K

Atepo, J

Unge, T

Hulten, J

Bonham, NM

Schaal, W

Karlen, A

Hallberg, A

机构：

[1] UPPSALA UNIV,BIOMED CTR,DEPT MOL BIOL,S-75124 UPPSALA,SWEDEN

[2] UPPSALA UNIV,BIOMED CTR,DEPT ORGAN PHARMACEUT CHEM,S-75123 UPPSALA,SWEDEN

来源：

JOURNAL OF MEDICINAL CHEMISTRY | 1997年 / 40卷 / 06期

关键词：

IMMUNODEFICIENCY-VIRUS PROTEASE; DEFICIENCY SYNDROME AIDS; X-RAY; CRYSTAL-STRUCTURE; RETROVIRAL PROTEASES; TYPE-1; PROTEASE; RESOLUTION; COMPLEX; DESIGN; TARGET;

D O I：

10.1021/jm960588d

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Two cyclic, C-2-symmetric HIV-1 protease inhibitors, one sulfamide and one urea derivative, both comprising phenyl ether groups in the P1/P1' positions were cocrystallized with HIV-1 protease, and the crystal structures were determined to 2.0 Angstrom resolution. The structure of the urea 2 showed a conformation similar to that reported for the related urea 3 by Lam et al., while the sulfamide 1 adopted an unanticipated conformation in which the P1' and P2' side chains were transposed.

引用

页码：898 / 902

页数：5

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