2K48

NMR Structure of the N-terminal Coiled Coil Domain of the Andes Hantavirus Nucleocapsid Protein

Summary for 2K48

• Entry DOI: 10.2210/pdb2k48/pdb
• NMR Information: BMRB: 15790
• Descriptor: Nucleoprotein (1 entity in total)
• Functional Keywords: viral nucleoprotein, viral protein
• Biological source: Andes virus
• Total number of polymer chains: 1
• Total formula weight: 12071.61

Authors

Wang, Y.,Boudreaux, D.M.,Estrada, D.F.,Egan, C.W.,St Jeor, S.C.,De Guzman, R.N. (deposition date: 2008-05-30, release date: 2008-08-05, Last modification date: 2024-05-29)

Primary citation

Wang, Y.,Boudreaux, D.M.,Estrada, D.F.,Egan, C.W.,St Jeor, S.C.,De Guzman, R.N.
NMR Structure of the N-terminal Coiled Coil Domain of the Andes Hantavirus Nucleocapsid Protein.
J.Biol.Chem., 283:28297-28304, 2008

PubMed Abstract: The hantaviruses are emerging infectious viruses that in humans can cause a cardiopulmonary syndrome or a hemorrhagic fever with renal syndrome. The nucleocapsid (N) is the most abundant viral protein, and during viral assembly, the N protein forms trimers and packages the viral RNA genome. Here, we report the NMR structure of the N-terminal domain (residues 1-74, called N1-74) of the Andes hantavirus N protein. N1-74 forms two long helices (alpha1 and alpha2) that intertwine into a coiled coil domain. The conserved hydrophobic residues at the helix alpha1-alpha2 interface stabilize the coiled coil; however, there are many conserved surface residues whose function is not known. Site-directed mutagenesis, CD spectroscopy, and immunocytochemistry reveal that a point mutation in the conserved basic surface formed by Arg22 or Lys26 lead to antibody recognition based on the subcellular localization of the N protein. Thus, Arg22 and Lys26 are likely involved in a conformational change or molecular recognition when the N protein is trafficked from the cytoplasm to the Golgi, the site of viral assembly and maturation.

PubMed: 18687679
DOI: 10.1074/jbc.M804869200

Experimental method

SOLUTION NMR