Unknown

Dataset Information

0

Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES.


ABSTRACT: The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV) encodes the conserved macro domain within non-structural protein 3. However, the precise biochemical function and structure of the macro domain is unclear. Using differential scanning fluorimetry and isothermal titration calorimetry, we characterized the MERS-CoV macro domain as a more efficient adenosine diphosphate (ADP)-ribose binding module than macro domains from other CoVs. Furthermore, the crystal structure of the MERS-CoV macro domain was determined at 1.43-Å resolution in complex with ADP-ribose. Comparison of macro domains from MERS-CoV and other human CoVs revealed structural differences in the ?1 helix alters how the conserved Asp-20 interacts with ADP-ribose and may explain the efficient binding of the MERS-CoV macro domain to ADP-ribose. This study provides structural and biophysical bases to further evaluate the role of the MERS-CoV macro domain in the host response via ADP-ribose binding but also as a potential target for drug design.

SUBMITTER: Cho CC 

PROVIDER: S-EPMC4777827 | BioStudies | 2016-01-01

REPOSITORIES: biostudies

Similar Datasets

2021-01-01 | S-EPMC7840908 | BioStudies
2020-01-01 | S-EPMC7537548 | BioStudies
2006-01-01 | S-EPMC1563857 | BioStudies
2005-01-01 | S-EPMC1142602 | BioStudies
2009-01-01 | S-EPMC7094737 | BioStudies
2009-01-01 | S-EPMC2698539 | BioStudies
2020-01-01 | S-EPMC7105881 | BioStudies
2016-01-01 | S-EPMC5021415 | BioStudies
2016-01-01 | S-EPMC5156301 | BioStudies
2006-01-01 | S-EPMC2222557 | BioStudies