2k9h | pdb_00002k9h

The hantavirus glycoprotein G1 tail contains a dual CCHC-type classical zinc fingers

spinqualitylabelsall models 2k9h, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k9h is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers.,Estrada DF, Boudreaux DM, Zhong D, St Jeor SC, De Guzman RN J Biol Chem. 2009 Mar 27;284(13):8654-60. Epub 2009 Jan 29. PMID:19179334 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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