Structural highlights
9b2h is a 2 chain structure with sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Method: | X-ray diffraction, Resolution 1.32Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q5RZ08_9HIV1
Publication Abstract from PubMed
Substituted tetrahydrofuran derivatives were designed and synthesized to serve as the P2 ligand for a series of potent HIV-1 protease inhibitors. Both enantiomers of the tetrahydrofuran derivatives were synthesized stereoselectivity in optically active forms using lipase-PS catalyzed enzymatic resolution as the key step. These tetrahydrofuran derivatives are designed to promote hydrogen bonding and van der Waals interactions with the backbone atoms in the S2 subsite of the HIV-1 protease active site. Several inhibitors displayed very potent HIV-1 protease inhibitory activity. A high-resolution X-ray crystal structure of an inhibitor-bound HIV-1 protease provided important insight into the ligand binding site interactions in the active site.
Design of substituted tetrahydrofuran derivatives for HIV-1 protease inhibitors: synthesis, biological evaluation, and X-ray structural studies.,Ghosh AK, Lee D, Sharma A, Johnson ME, Ghosh AK, Wang YF, Agniswamy J, Amano M, Hattori SI, Weber IT, Mitsuya H Org Biomol Chem. 2024 Jul 8. doi: 10.1039/d4ob00506f. PMID:38973505[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghosh AK, Lee D, Sharma A, Johnson ME, Ghosh AK, Wang YF, Agniswamy J, Amano M, Hattori SI, Weber IT, Mitsuya H. Design of substituted tetrahydrofuran derivatives for HIV-1 protease inhibitors: synthesis, biological evaluation, and X-ray structural studies. Org Biomol Chem. 2024 Jul 8. PMID:38973505 doi:10.1039/d4ob00506f
