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Literature summary for 3.4.23.B11 extracted from

  • Hartl, M.J.; Bodem, J.; Jochheim, F.; Rethwilm, A.; Roesch, P.; Woehrl, B.M.
    Regulation of foamy virus protease activity by viral RNA: a novel and unique mechanism among retroviruses (2011), J. Virol., 85, 4462-4469.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.B11

Activating Compound

Activating Compound Comment Organism Structure
additional information identification of a specific protease-activating RNA motif PARM located in the pol region of viral RNA, which stimulates protease activity in vitro and in vivo. PARM spans the A and B regions of the central purine-rich sequences of the prototype foamy virus (pre)genomic RNA. PARM enables foamy virus protease-reverse transcriptase to form a proteolytically active dimer in vitro as well as in vivo. At least two foamy virus protease-reverse transcriptase molecules bind to the PARM and only RNAs containing the PARM result in significant activation of the protease. DNA harboring the PARM is not capable of protease activation.The PARM displays a distinct RNA folding, important for protease activation and thus virus maturation Simian foamy virus

Organism

Organism UniProt Comment Textmining
Simian foamy virus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GB1-GFP + H2O peptide substrate, harboring the simian foamy virus mac reverse transcriptase-viral integrase cleavage site of the Pol polyprotein, ATQGSYVVHCNTTP, between immunoglobulin binding domain B1 of streptococcal protein G, GB1, and green fluorescent protein,GFP Simian foamy virus ?
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Subunits

Subunits Comment Organism
dimer protease is an inactive monomer which forms an active dimer upon binding to protease-activating RNA motif PARM Simian foamy virus
monomer protease is an inactive monomer which forms an active dimer upon binding to protease-activating RNA motif PARM Simian foamy virus