2K9H
The hantavirus glycoprotein G1 tail contains a dual CCHC-type classical zinc fingers
Summary for 2K9H
| Entry DOI | 10.2210/pdb2k9h/pdb |
| Descriptor | Glycoprotein, ZINC ION (2 entities in total) |
| Functional Keywords | hantavirus, glycoprotein, zinc finger, cchc, metal binding protein |
| Biological source | Andes virus |
| Total number of polymer chains | 1 |
| Total formula weight | 6475.06 |
| Authors | Estrada, D.F.,Boudreaux, D.M.,Zhong, D.,St Jeor, S.C.,De Guzman, R.N. (deposition date: 2008-10-13, release date: 2009-01-27, Last modification date: 2024-05-22) |
| Primary citation | Estrada, D.F.,Boudreaux, D.M.,Zhong, D.,St Jeor, S.C.,De Guzman, R.N. The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers. J.Biol.Chem., 284:8654-8660, 2009 Cited by PubMed Abstract: Hantaviruses are distributed worldwide and can cause a hemorrhagic fever or a cardiopulmonary syndrome in humans. Mature virions consist of RNA genome, nucleocapsid protein, RNA polymerase, and two transmembrane glycoproteins, G1 and G2. The ectodomain of G1 is surface-exposed; however, it has a 142-residue C-terminal cytoplasmic tail that plays important roles in viral assembly and host-pathogen interaction. Here we show by NMR, circular dichroism spectroscopy, and mutagenesis that a highly conserved cysteine/histidine-rich region in the G1 tail of hantaviruses forms two CCHC-type classical zinc fingers. Unlike classical zinc fingers, however, the two G1 zinc fingers are intimately joined together, forming a compact domain with a unique fold. We discuss the implication of the hantaviral G1 zinc fingers in viral assembly and host-pathogen interaction. PubMed: 19179334DOI: 10.1074/jbc.M808081200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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