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Literature summary for 3.4.22.B79 extracted from

  • Shin, G.; Yost, S.A.; Miller, M.T.; Elrod, E.J.; Grakoui, A.; Marcotrigiano, J.
    Structural and functional insights into alphavirus polyprotein processing and pathogenesis (2012), Proc. Natl. Acad. Sci. USA, 109, 16534-16539.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of nonstructural protein P23 in a precleavage form. The proteins form an extensive interface and nsP3 creates a ring structure that encircles nsP2. The P2/3 cleavage site is located at the base of a narrow cleft and is not readily accessible. The nsP2 protease active site is over 40 A away from the P2/3 cleavage site, supporting a trans cleavage mechanism. nsP3 contains a previously uncharacterized protein fold with a zinc-coordination site. Known mutations in nsP2 that result in formation of noncytopathic viruses or a temperature sensitive phenotype cluster at the nsP2/nsP3 interface Sindbis virus

Organism

Organism UniProt Comment Textmining
Sindbis virus P03317
-
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification nonstructural proteins nsP1-4 are produced as a single polyprotein, and processing of the polyprotein occurs in a highly regulated manner. The P2/3 cleavage site is located at the base of a narrow cleft and is not readily accessible. The nsP2 protease active site is over 40 A away from the P2/3 cleavage site, supporting a trans cleavage mechanism Sindbis virus