8V0H

Structural characterization of zika virus NS2B by NMR and RosettaMP

Summary for 8V0H

• Entry DOI: 10.2210/pdb8v0h/pdb
• NMR Information: BMRB: 50994
• Descriptor: Serine protease subunit NS2B (1 entity in total)
• Functional Keywords: ns2b, membrane protein, viral replication, ns3 protease cofactor, viral protein
• Biological source: Zika virus
• Total number of polymer chains: 1
• Total formula weight: 17085.57

Authors

Penna, B.R.,Gomes-Neto, F.,Anobom, C.D.,Valente, A.P. (deposition date: 2023-11-17, release date: 2024-10-16)

Primary citation

Penna, B.R.,Gomes-Neto, F.,Anobom, C.D.,Valente, A.P.
Structural and dynamics characterization of the Zika virus NS2B using nuclear magnetic resonance and RosettaMP: A challenge for transmembrane protein studies.
Int.J.Biol.Macromol., 280:136074-136074, 2024

PubMed Abstract: Zika virus (ZIKV) is an emergent flavivirus that represents a global public health concern due to its association with severe neurological disorders. NS2B is a multifunctional viral membrane protein primarily used to regulate viral protease activity and is crucial for virus replication, making it an appealing target for antiviral drugs. This study presents the structural elucidation of full-length ZIKV NS2B in sodium dodecyl sulfate (SDS) micelles using solution nuclear magnetic resonance experimental data and RosettaMP. The protein structure has four transmembrane α-helices, two amphipathic α-helices, and a β-hairpin in the hydrophilic region. NS2B presented secondary and tertiary stability in different concentrations of SDS. Furthermore, we studied the dynamics of NS2B in SDS micelles through relaxation parameters and paramagnetic relaxation enhancement experiments. The findings were consistent with the structural calculations. Our work will be essential in understanding the role of NS2B in viral replication and screening for inhibitors against ZIKV.

PubMed: 39341314
DOI: 10.1016/j.ijbiomac.2024.136074

Experimental method

SOLUTION NMR