Hemagglutinin-esterase

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Template:STRUCTURE 3i1l

Contents 1 Function 2 Structural highlights 3 3D structures of hemagglutinin-esterase 4 References

Function

Hemagglutinin-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 highlights

The HE is a trimer and each monomer contains 3 domains: the membrane fusion domain, the esterase domain and the receptor-binding domain. The receptor binding site of HE is located at five exposed surface loops. HE contains a conserved metal-binding site^[2].

3D structures of hemagglutinin-esterase

Updated on 21-March-2016

3cl4 – bHE – bovine
3cl5 – bHE (mutant) + receptor
3i1k – PtHE (mutant) – porcine torovirus
3i1l – PtHE (mutant) + receptor
3i26 – BtHE – bovine torovirus
3i27 – BtHE + receptor
4c7l – mhvHE (mutant) – murine hepatitis virus
4c7w – mhvHE (mutant) + receptor

References

1. ↑ 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
2. ↑ 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