| Title | C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer |
| Authors | Zhong, Nan Zhang, Shengnan Xue, Fei Kang, Xue Zou, Peng Chen, Jiaxuan Liang, Chao Rao, Zihe Jin, Changwen Lou, Zhiyong Xia, Bin |
| Affiliation | Tsinghua Univ, Struct Biol Lab, Beijing 100084, Peoples R China. Peking Univ, Beijing Nucl Magnet Resonance Ctr, Beijing 100871, Peoples R China. Peking Univ, Coll Chem & Mol Engn, Beijing 100871, Peoples R China. Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China. |
| Keywords | SARS main protease domain-swapping dimerization C-terminal domain ACUTE RESPIRATORY SYNDROME TORSION ANGLE DYNAMICS CHEMICAL-SHIFT INDEX MACROMOLECULAR STRUCTURES SYNDROME CORONAVIRUS SECONDARY STRUCTURE PROTEINASE ASSIGNMENT SOFTWARE REVEALS |
| Issue Date | 2009 |
| Publisher | 蛋白质科学 |
| Citation | PROTEIN SCIENCE.2009,18,(4),839-844. |
| 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)-Delta 7) 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)-Delta 7. |
| URI | http://hdl.handle.net/20.500.11897/150179 |
| ISSN | 0961-8368 |
| DOI | 10.1002/pro.76 |
| Indexed | SCI(E) PubMed |
| Appears in Collections: | å å¦ä¸ å å å·¥ç¨ å¦é ¢ 生命科学学院 |
