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Structure paper

TitleMinor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition
Journal, issue, pagesFebs Lett., Vol. 583, Page 235-240, Year 2009
Publish dateJul 9, 2008 (structure data deposition date)
AuthorsQuerol-Audi, J. / Konecsni, T. / Pous, J. / Carugo, O. / Fita, I. / Verdaguer, N. / Blaas, D.
External linksFebs Lett. / PubMed:19073182
MethodsX-ray diffraction
Resolution3.5 Å
Structure data

PDB-3dpr:
Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

Chemicals

ChemComp-DAO:
LAURIC ACID

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • human rhinovirus 2
KeywordsVIRUS / HUMAN RHINOVIRUS / VLDL-RECEPTOR / VIRUS-PROTEIN COMPLEX / ICOSAHEDRAL VIRUS / ATP-binding / Capsid protein / Covalent protein-RNA linkage / Cytoplasmic vesicle / Helicase / Host-virus interaction / Hydrolase / Lipoprotein / Membrane / Myristate / Nucleotide-binding / Nucleotidyltransferase / Phosphoprotein / Protease / RNA replication / RNA-binding / RNA-directed RNA polymerase / Thiol protease / Transferase / Virion / Cholesterol metabolism / Coated pit / EGF-like domain / Endocytosis / Glycoprotein / Lipid metabolism / Lipid transport / Receptor / Steroid metabolism / Transmembrane / Transport / VLDL

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