Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.23.16 extracted from

  • Liu, X.; Xiu, Z.; Hao, C.
    Drug-resistant molecular mechanism of CRF01_AE HIV-1 protease due to V82F mutation (2009), J. Comput. Aided Mol. Des., 23, 261-272.
    View publication on PubMed
Search for more literature for 3.4.23.16

Crystallization (Commentary)

Crystallization (Comment) Organism
computer simulation of subtype AE HIV-1 protease with the drugs lopinavir and nelfinavir. Comparison of the interactive mechanisms of lopinavir and nelfinavir with HIV-1 protease shows that the presence of a dodecahydroisoquinoline ring at the P10 subsite, a [2-(2,6-dimethylphenoxy)acetyl]amino group at the P20 subsite, and an N2 atom at the P2 subsite could improve the binding affinity of the drug with AE HIV-1 protease Human immunodeficiency virus 1

Protein Variants

Protein Variants Comment Organism
V82F mutation at the active site resulting in a conformational change of 79's loop region and displacement of inhibitor lopinavir from its proper binding site, changes lead to rotation of the side-chains of residues D25 and I50'. The conformation of the binding cavity is deformed asymmetrically and some interactions between protease and lopinavir are destroyed Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
lopinavir computer simulation of comlex with HIV-1 protease Human immunodeficiency virus 1
nelfinavir computer simulation of comlex with HIV-1 protease Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
-
-