Structural highlights
Function
A0A3S8UVN5_9MONO
Publication Abstract from PubMed
The family Filoviridae contains many important human viruses, including Marburg virus (MARV) and Ebola virus (EBOV). Mengla virus (MLAV), a newly discovered filovirus, is considered a potential human pathogen. The VP30 C-terminal domain (CTD) of these filoviruses plays an essential role in virion assembly. In common with other filoviruses, MLAV VP30 CTD mainly exists as a dimer in solution. In this work, we determined the crystal structure of recombinant MLAV VP30 CTD monomer, verifying that C-terminal helix-7 (H7) is critical for the dimerization process. This study provides a preliminary model for investigation of MLAV VP30 CTD as an anti-filovirus drug development target.
Crystal structure of the Mengla virus VP30 C-terminal domain.,Dong S, Wen K, Chu H, Li H, Yu Q, Wang C, Qin X Biochem Biophys Res Commun. 2020 Apr 30;525(2):392-397. doi: , 10.1016/j.bbrc.2020.02.089. Epub 2020 Feb 22. PMID:32093889[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dong S, Wen K, Chu H, Li H, Yu Q, Wang C, Qin X. Crystal structure of the Měnglà virus VP30 C-terminal domain. Biochem Biophys Res Commun. 2020 Apr 30;525(2):392-397. PMID:32093889 doi:10.1016/j.bbrc.2020.02.089
