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Structure paper

TitleStructural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies.
Journal, issue, pagesPlos Pathog., Vol. 8, Page e1002859-e1002859, Year 2012
Publish dateMay 8, 2012 (structure data deposition date)
AuthorsReguera, J. / Santiago, C. / Mudgal, G. / Ordono, D. / Enjuanes, L. / Casasnovas, J.M.
External linksPlos Pathog. / PubMed:22876187
MethodsX-ray diffraction
Resolution3 - 3.2 Å
Structure data

PDB-4f2m:
Crystal structure of a TGEV coronavirus Spike fragment in complex with the TGEV neutralizing monoclonal antibody 1AF10
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-4f5c:
Crystal structure of the spike receptor binding domain of a porcine respiratory coronavirus in complex with the pig aminopeptidase N ectodomain
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-ACY:
ACETIC ACID

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

Source
  • mus musculus (house mouse)
  • tgev virulent purdue (virus)
  • sus scrofa (pig)
  • porcine respiratory coronavirus
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / beta-barrel / immunoglobulin / virus entry / virus neutralization / cellular receptor / aminopeptidase N / glycosylation / virus membrane / VIRAL PROTEIN-IMMUNE SYSTEM complex / HYDROLASE/VIRAL PROTEIN / metalloprotease / HYDROLASE-VIRAL PROTEIN complex

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