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10.1002/pro.76

http://scihub22266oqcxt.onion/10.1002/pro.76
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19319935!2762595!19319935
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suck abstract from ncbi


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pmid19319935      Protein+Sci 2009 ; 18 (4): 839-44
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  • C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer #MMPMID19319935
  • Zhong N; Zhang S; Xue F; Kang X; Zou P; Chen J; Liang C; Rao Z; Jin C; Lou Z; Xia B
  • Protein Sci 2009[Apr]; 18 (4): 839-44 PMID19319935show ga
  • SARS coronavirus main protease (M(pro)) plays an essential role in the extensive proteolytic processing of the viral polyproteins (pp1a and pp1ab), and it is an important target for anti-SARS drug development. We have reported that both the M(pro) C-terminal domain alone (M(pro)-C) and the N-finger deletion mutant of M(pro) (M(pro)-Delta7) exist as a stable dimer and a stable monomer (Zhong et al., J Virol 2008; 82:4227-4234). Here, we report structures of both M(pro)-C monomer and dimer. The structure of the M(pro)-C monomer is almost identical to that of the C-terminal domain in the crystal structure of M(pro). Interestingly, the M(pro)-C dimer structure is characterized by 3D domain-swapping, in which the first helices of the two protomers are interchanged and each is enwrapped by four other helices from the other protomer. Each folding subunit of the M(pro)-C domain-swapped dimer still has the same general fold as that of the M(pro)-C monomer. This special dimerization elucidates the structural basis for the observation that there is no exchange between monomeric and dimeric forms of M(pro)-C and M(pro)-Delta7.
  • |Coronavirus 3C Proteases[MESH]
  • |Crystallography, X-Ray[MESH]
  • |Cysteine Endopeptidases/*chemistry/metabolism[MESH]
  • |Humans[MESH]
  • |Protein Conformation[MESH]
  • |Protein Multimerization[MESH]
  • |Protein Structure, Tertiary[MESH]
  • |Severe acute respiratory syndrome-related coronavirus/*enzymology[MESH]
  • |Viral Core Proteins/*chemistry/metabolism[MESH]


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