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Literature summary for 3.4.23.B10 extracted from

  • Schur, F.K.; Dick, R.A.; Hagen, W.J.; Vogt, V.M.; Briggs, J.A.
    The structure of immature virus-like Rous sarcoma virus Gag particles reveals a structural role for the p10 domain in assembly (2015), J. Virol., 89, 10294-10302 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.B10

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required Rous sarcoma virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rous sarcoma virus the enzyme cleaves the RSV Gag protein and virus-like particles (VLPs) ?
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 ?

Organism

Organism UniProt Comment Textmining
Rous sarcoma virus
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 RSV
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme cleaves the RSV Gag protein and virus-like particles (VLPs) Rous sarcoma virus ?
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 ?
additional information the enzyme cleaves the RSV Gag protein and virus-like particles (VLPs). Structure determination of in vitro-assembled, immature virus-like Rous sarcoma virus (RSV) Gag particles, overview Rous sarcoma virus ?
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 ?

Synonyms

Synonyms Comment Organism
viral protease
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 Rous sarcoma virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Rous sarcoma virus

General Information

General Information Comment Organism
additional information the C-terminal domain of RSV conserved capsid (CA) is arranged similarly to HIV-1 and M-PMV, whereas the N-terminal domain of CA adopts a novel arrangement in which the upstream p10 domain folds back into the CA lattice. In this position the cleavage site between CA and p10 appears to be inaccessible to the protease. Below CA, an extended density is consistent with the presence of a six-helix bundle formed by the spacer-peptide region. The cleavage between p10 and CA is indeed inhibited in the assembled lattice, a finding consistent with structural regulation of proteolytic maturation. Docking study and molecular dynamics flexible fitting. The major interaction across the dimeric interface occurs between adjacent hexamers at the CA-CTD is in the region of hydrophobic residues Pro426 and Val427 in helix 9. RSV has a cysteine residue (Cys431) at the base of helix 9 that has been speculated to participate in the interaction across the CA-CTD dimer interface. Modelling shows that the distance between Cys431 residues across the dimer interface is too large to permit disulfide bridge formation in the immature particle Rous sarcoma virus
physiological function proteolytic cleavage of Gag by the viral protease (PR) is required for maturation of retroviruses from an immature form into an infectious form. Gag is cleaved by the viral protease enzyme into separate domains, leading to rearrangement of the virus into its infectious form Rous sarcoma virus