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Crystal structure of the Mengla Virus VP30 C-terminal domain
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Structural highlights
FunctionPublication Abstract from PubMedThe 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
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This page was last modified 14:54, 29 November 2023.