ArticleProtein science : a publication of the Protein Society2003
Kinetics of the dimerization of retroviral proteases: the "fireman's grip" and dimerization.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 31 citations in OpenAlex.
- Structural Catalytic Core of the Members of the Superfamily of Acid Proteases.Molecules (Basel, Switzerland) · 2024Review
- Kinetics of Bovine leukemia virus aspartic protease reveals its dimerization and conformational change.PloS one · 2022Article
- Precursors of Viral Proteases as Distinct Drug Targets.Viruses · 2021Review
- Chemically functionalized conical PET nanopore for protein detection at the single-molecule level.Biosensors & bioelectronics · 2020Article
- Dimer Interface Organization is a Main Determinant of Intermonomeric Interactions and Correlates with Evolutionary Relationships of Retroviral and Retroviral-Like Ddi1 and Ddi2 Proteases.International journal of molecular sciences · 2020Article
- Protease-Activatable Scaffold Proteins as Versatile Molecular Hubs in Synthetic Signaling Networks.ACS synthetic biology · 2018Article
- Graphene oxide-based biosensing platform for rapid and sensitive detection of HIV-1 protease.Analytical and bioanalytical chemistry · 2018Article
- NS2 proteases from hepatitis C virus and related hepaciviruses share composite active sites and previously unrecognized intrinsic proteolytic activities.PLoS pathogens · 2018Article
- Plant Viral Proteases: Beyond the Role of Peptide Cutters.Frontiers in plant science · 2018Review
- Inhibitors Alter the Stochasticity of Regulatory Proteins to Force Cells to Switch to the Other State in the Bistable System.Scientific reports · 2017Article
- Four Amino Acid Changes in HIV-2 Protease Confer Class-Wide Sensitivity to Protease Inhibitors.Journal of virology · 2016Article
- Fluorogenic Assay for Inhibitors of HIV-1 Protease with Sub-picomolar Affinity.Scientific reports · 2015Article
- Article
- A multi-drug resistant HIV-1 protease is resistant to the dimerization inhibitory activity of TLF-PafF.Journal of molecular graphics & modelling · 2014Article
- Ramachandran analysis of conserved glycyl residues in homologous proteins of known structure.Protein science : a publication of the Protein Society · 2014Article
- Avian oncogenesis induced by lymphoproliferative disease virus: a neglected or emerging retroviral pathogen?Virology · 2014Article
- Current and Novel Inhibitors of HIV Protease.Viruses · 2009Article
- Molecular dynamics studies on HIV-1 protease: a comparison of the flap motions between wild type protease and the M46I/G51D double mutant.Journal of molecular modeling · 2007Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All retroviral proteases belong to the family of aspartic proteases. They are active as homodimers, each unit contributing one catalytic aspartate to the active site dyad. An important feature of all aspartic proteases is a conserved complex scaffold of hydrogen bonds supporting the active site, called the "fireman's grip," which involves the hydroxyl groups of two threonine (serine) residues in the active site Asp-Thr(Ser)-Gly triplets. It was shown previously that the fireman's grip is indispensable for the dimer stability of HIV protease. The retroviral proteases harboring Ser in their active site triplet are less active and, under natural conditions, are expressed in higher enzyme/substrate ratio than those having Asp-Thr-Gly triplet. To analyze whether this observation can be attributed to the different influence of Thr or Ser on dimerization, we prepared two pairs of the wild-type and mutant proteases from HIV and myeloblastosis-associated virus harboring either Ser or Thr in their Asp-Thr(Ser)-Gly triplet. The equilibrium dimerization constants differed by an order of magnitude within the relevant pairs. The proteases with Thr in their active site triplets were found to be approximately 10 times more thermodynamically stable. The dimer association contributes to this difference more than does the dissociation. We propose that the fireman's grip might be important in the initial phases of dimer formation to help properly orientate the two subunits of a retroviral protease. The methyl group of threonine might contribute significantly to fixing such an intermediate conformation.
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