Literature summary for 3.4.22.B79 extracted from

Russo, A.T.; Malmstrom, R.D.; White, M.A.; Watowich, S.J.
Structural basis for substrate specificity of alphavirus nsP2 proteases (2010), J. Mol. Graph. Model., 29, 46-53.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
combination of molecular dynamics simulations with structural studies. The catalytic mechanism of the nsP2 protease appears similar to the papain-like cysteine proteases, with the conserved catalytic dyad forming a thiolate-imidazolium ion pair in the nsP2-activated state. Substrate binding likely stabilizes this ion pair. Protease residues His510, Ser511, His546, and Lys706 are critical for cleavage site recognition. Structural determinants of substrate specificity that recognize features common to all three cleavage sites within the viral polyprotein are strongly conserved among alphaviruses. Contacts between S2/P2 and S3/P3 residues illustrate preserved binding motifs such as the ubiquitous P2 glycine interaction with Trp547 and hydrogen bonding between P2 and His510	Venezuelan equine encephalitis virus

Crystallization (Comment)

Organism

combination of molecular dynamics simulations with structural studies. The catalytic mechanism of the nsP2 protease appears similar to the papain-like cysteine proteases, with the conserved catalytic dyad forming a thiolate-imidazolium ion pair in the nsP2-activated state. Substrate binding likely stabilizes this ion pair. Protease residues His510, Ser511, His546, and Lys706 are critical for cleavage site recognition. Structural determinants of substrate specificity that recognize features common to all three cleavage sites within the viral polyprotein are strongly conserved among alphaviruses. Contacts between S2/P2 and S3/P3 residues illustrate preserved binding motifs such as the ubiquitous P2 glycine interaction with Trp547 and hydrogen bonding between P2 and His510

Venezuelan equine encephalitis virus

Organism

Organism	UniProt	Comment	Textmining
Venezuelan equine encephalitis virus	P27282	-	-

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Release 2023.1 (January 2023)