2K7X

solution structure of C-terminal domain of SARS-CoV main protease

2K7X の概要

• エントリーDOI: 10.2210/pdb2k7x/pdb
• 分子名称: SARS-CoV main protease (1 entity in total)
• 機能のキーワード: solution structure, c-terminal domain, main protease, hydrolase
• 由来する生物種: SARS coronavirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13282.98

構造登録者

Xia, B.,Zhong, N. (登録日: 2008-08-28, 公開日: 2009-05-12, 最終更新日: 2024-05-22)

主引用文献

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.
Protein Sci., 18:839-844, 2009

PubMed Abstract: 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.

PubMed: 19319935
DOI: 10.1002/pro.76

実験手法

SOLUTION NMR