Hemagglutinin-esterase

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{{STRUCTURE_3i1l| PDB=3i1l | SIZE=400| SCENE= |right|CAPTION=Pig glycosylated hemagglutinin-esterase glycoprotein complex with receptor and acetate [[3i1l]]}}
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{{STRUCTURE_3i1l| PDB=3i1l | SIZE=400| SCENE= |right|CAPTION=Pig torovirus glycosylated hemagglutinin-esterase glycoprotein complex with receptor and acetate [[3i1l]]}}
== Function ==
== Function ==

Revision as of 12:03, 20 March 2016

Template:STRUCTURE 3i1l

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]. The HE is a trimer and each monomer contains 3 domains: the membrane fusion domain, the esterase domain and the receptor-binding domain.

3D structures of hemagglutinin-esterase

Updated on 20-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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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