2k9h | pdb_00002k9h
The hantavirus glycoprotein G1 tail contains a dual CCHC-type classical zinc fingers
Structural highlights
FunctionGP_ANDV Forms homotetramers with glycoprotein C at the surface of the virion (By similarity). Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (By similarity). This attachment induces virion internalization possibly through clathrin-dependent endocytosis and dynamin-independent macropinocytosis (Probable). Mediates the assembly and budding of infectious virus particles through its interaction with the nucleocapsid protein and the viral genome (By similarity). May dysregulate normal immune and endothelial cell responses through an ITAM motif (By similarity). Translocates to mitochondria, binds to host TUFM and recruits MAP1LC3B (By similarity). These interactions induce mitochondrial autophagy and therefore destruction of host MAVS leading to inhibition of type I interferon (IFN) responses (By similarity). Concomitant breakdown of glycoprotein N is apparently prevented by the nucleoprotein that may inhibit Gn-stimulated autophagosome-lysosome fusion (By similarity). Interacts with the viral genomic RNA (By similarity). Inhibits the host RIG-I/TBK1 pathway by disrupting the formation of TBK1-TRAF3 complexes and downstream signaling responses required for IFN-beta transcription (PubMed:24390324, PubMed:16973572).[UniProtKB:P08668][UniProtKB:P27312][1] [2] Forms homotetramers with glycoprotein N at the surface of the virion. Attaches the virion to host cell receptors including integrin ITGAV/ITGB3. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity). Class II fusion protein that promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion (PubMed:31180319, PubMed:27414047).[UniProtKB:P08668][3] [4] 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 PubMedHantaviruses 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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