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Structural analysis of HIV‐1 protease inhibition using physical models
Author(s) -
Colton Shan,
Herman Tim,
Giles Kurt,
Koo Ben,
Jeske Sabine,
Ollikainen Noah,
Reis Julie
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.837.5
Subject(s) - human immunodeficiency virus (hiv) , protease , virology , viral replication , hiv 1 protease , computational biology , drug , medicine , biology , virus , enzyme , pharmacology , biochemistry
HIV‐1 protease (HIV PR) is an essential enzyme for HIV replication. HIV PR cleaves immature HIV polypeptides resulting in the active protein components required for an infectious virus. Numerous HIV PR inhibitors have been developed in order to prevent and treat HIV infection, however, the rapid evolution of HIV PR has allowed HIV to become drug resistant and remain infectious. Here we examine the inhibition of HIV PR from a structural perspective by building physical 3D models of HIV PR variants in complex with different inhibitors. These models allow us to analyze the key interactions that enable the inhibition of HIV PR and provide us with visual tools for studying the structural basis of drug resistance mutations. The SMART (Students Modeling A Research Topic) program was established by the Center of BioMolecular Modeling at the Milwaukee School of Engineering and involves partnerships between university researchers and local high schools. This work is funded by NIH‐NCRR‐SEPA and HHMI.