Αποτελέσματα Αναζήτησης
The X-ray crystal structure of a core HIV-1 gp120 construct revealed the 3D fold of the critical viral glycoprotein as well as details of its interaction with the cell CD4 receptor and a neutralizing antibody.
A cell-derived lipid membrane surrounds the viron, with ~30 viral "spikes" distributed on its surface (left in expanded image), whereas host proteins on its surface include the major histocompatibility complex class II molecules (e.g., HLA-DR1) that increase HIV infectivity by binding CD4 on T cells.
Structure of HIV Protease. HIV protease begins as a component of the Gag/Pol fusion polyprotein. As a single molecule, the Gag/Pol-embedded protease is inactive, because dimer formation is required to create the active site and catalytic machinery.
The proteins in HIV are built as long polyproteins, which then must be cleaved into the proper functional pieces by HIV protease. Protease inhibitors are widely used as anti-HIV drugs, often in combination with drugs that block reverse transcriptase and integrase.
Knowledge of the crystal structure of HIV-1 protease and its recognition of substrate analog inhibitors was critical for the design of antiviral PIs. The HIV protease is an aspartic protease and the catalytic site has the characteristic Asp-Thr-Gly sequence common to all aspartic proteases.
16 Μαρ 2012 · HIV-1 replication relies on the proper functioning of specific viral proteins, three of which — protease, integrase, and reverse transcriptase with associated RNase H activity — are enzymes.
11 Νοε 2008 · Our analysis identified residues both in the hydrophobic core and at the dimeric interface (DI) that are very important for the protease function. This study demonstrates a potential utility of the SNAPP method for rational design of mutagenesis studies and protein engineering.
