Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
New World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor. This first structure of an arenavirus glycoprotein shows that GP1 consists of a novel alpha/beta fold. This provides a blueprint of the New World arenavirus attachment glycoproteins and reveals a new architecture of viral attachment, using a protein fold of unknown origins.
Unusual molecular architecture of the machupo virus attachment glycoprotein.,Bowden TA, Crispin M, Graham SC, Harvey DJ, Grimes JM, Jones EY, Stuart DI J Virol. 2009 Aug;83(16):8259-65. Epub 2009 Jun 3. PMID:19494008[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bowden TA, Crispin M, Graham SC, Harvey DJ, Grimes JM, Jones EY, Stuart DI. Unusual molecular architecture of the machupo virus attachment glycoprotein. J Virol. 2009 Aug;83(16):8259-65. Epub 2009 Jun 3. PMID:19494008 doi:10.1128/JVI.00761-09
