Hemagglutinin-esterase: Difference between revisions
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Latest revision as of 11:23, 24 July 2019
FunctionHemagglutinin-esterase (HE) is a glycoprotein of the envelopes of some viruses. HE recognizes the host cell surface receptor - a sialic acid derivative. The esterase region of the HE is responsible for the destruction of the receptor[1]. Structural highlightsThe biological assmebly of HE is a and each monomer contains . The receptor binding site of HE is located at five exposed surface loops. . HE contains a [2]. 3D structures of hemagglutinin-esteraseHemagglutinin-esterase 3D structures
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ReferencesReferences
- ↑ de Groot RJ. Structure, function and evolution of the hemagglutinin-esterase proteins of corona- and toroviruses. Glycoconj J. 2006 Feb;23(1-2):59-72. PMID:16575523 doi:http://dx.doi.org/10.1007/s10719-006-5438-8
- ↑ Langereis MA, Zeng Q, Heesters BA, Huizinga EG, de Groot RJ. The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture. PLoS Pathog. 2012 Jan;8(1):e1002492. doi: 10.1371/journal.ppat.1002492. Epub 2012, Jan 26. PMID:22291594 doi:http://dx.doi.org/10.1371/journal.ppat.1002492