Hemagglutinin-esterase

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{{STRUCTURE_3i1l| PDB=3i1l | SIZE=400| SCENE= |right|CAPTION=Porcine torovirus hemagglutinin-esterase glycoprotein complex with receptor [[3i1l]]}}
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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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Revision as of 10:33, 18 August 2014

Template:STRUCTURE 3i1l

Hemagglutinin-esterase (HE) is a glycoprotein of the envelopes of some viruses. HE recognizes the host cell surface receptor. The esterase region of the HE is responsible for the destruction of the receptor. 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 18-August-2014

3cl4 – bHE – bovine
3cl5 – bHE (mutant) + sialic acid derivative
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) + sialic acid

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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