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Literature summary for 3.4.22.69 extracted from

  • Zhong, N.; Zhang, S.; Xue, F.; Kang, X.; Zou, P.; Chen, J.; Liang, C.; Rao, Z.; Jin, C.; Lou, Z.; Xia, B.
    C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer (2009), Protein Sci., 18, 839-844.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
structures of monomeric and dimeric forms of the C-terminal domain of Mpro (Mpro-C). Mpro-C monomer maintains the same fold as that in the crystal structure of Mpro. On the other hand, the Mpro-C dimer has a novel structure characterized by 3D domain-swapping, which provides the structural basis for the dimer stability Severe acute respiratory syndrome-related coronavirus

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome-related coronavirus
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Synonyms

Synonyms Comment Organism
SARS-CoV main protease
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 Severe acute respiratory syndrome-related coronavirus