1R6R

Solution Structure of Dengue Virus Capsid Protein Reveals a New Fold

Summary for 1R6R

• Entry DOI: 10.2210/pdb1r6r/pdb
• Descriptor: Genome polyprotein (1 entity in total)
• Functional Keywords: alpha helical, dimer, viral protein
• Biological source: Dengue virus 2 Puerto Rico/PR159-S1/1969
• Cellular location: Capsid protein C: Virion (Potential). Peptide pr: Secreted (By similarity). Small envelope protein M: Virion membrane; Multi-pass membrane protein (By similarity). Envelope protein E: Virion membrane; Multi- pass membrane protein (By similarity). Non-structural protein 1: Secreted. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P12823
• Total number of polymer chains: 2
• Total formula weight: 23584.57

Authors

Ma, L.,Jones, C.T.,Groesch, T.D.,Kuhn, R.J.,Post, C.B. (deposition date: 2003-10-16, release date: 2004-02-17, Last modification date: 2024-05-22)

Primary citation

Ma, L.,Jones, C.T.,Groesch, T.D.,Kuhn, R.J.,Post, C.B.
Solution structure of dengue virus capsid protein reveals another fold
Proc.Natl.Acad.Sci.USA, 101:3414-3419, 2004

PubMed Abstract: Dengue virus is responsible for approximately 50-100 million infections, resulting in nearly 24,000 deaths annually. The capsid (C) protein of dengue virus is essential for specific encapsidation of the RNA genome, but little structural information on the C protein is available. We report the solution structure of the 200-residue homodimer of dengue 2 C protein. The structure provides, to our knowledge, the first 3D picture of a flavivirus C protein and identifies a fold that includes a large dimerization surface contributed by two pairs of helices, one of which has characteristics of a coiled-coil. NMR structure determination involved a secondary structure sorting approach to facilitate assignment of the intersubunit nuclear Overhauser effect interactions. The dimer of dengue C protein has an unusually high net charge, and the structure reveals an asymmetric distribution of basic residues over the surface of the protein. Nearly half of the basic residues lie along one face of the dimer. In contrast, the conserved hydrophobic region forms an extensive apolar surface at a dimer interface on the opposite side of the molecule. We propose a model for the interaction of dengue C protein with RNA and the viral membrane that is based on the asymmetric charge distribution of the protein and is consistent with previously reported results.

PubMed: 14993605
DOI: 10.1073/pnas.0305892101

Experimental method

SOLUTION NMR