3DPR

Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3

Summary for 3DPR

• Entry DOI: 10.2210/pdb3dpr/pdb
• Descriptor: Protein VP1, Protein VP2, Protein VP3, ... (7 entities in total)
• Functional Keywords: 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, virus
• Biological source: Homo sapiens (Human); More
• Cellular location: Capsid protein VP0: Virion . Capsid protein VP4: Virion . Capsid protein VP2: Virion . Capsid protein VP3: Virion . Capsid protein VP1: Virion . Protein 2B: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 2C: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3A: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3AB: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Viral protein genome-linked: Virion . Protease 3C: Host cytoplasm . Protein 3CD: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P04936 P04936 P04936 P04936; Membrane; Single-pass type I membrane protein: P98155
• Total number of polymer chains: 5
• Total formula weight: 99914.08

Authors

Querol-Audi, J.,Pous, J.,Fita, I.,Verdaguer, N. (deposition date: 2008-07-09, release date: 2009-04-07, Last modification date: 2024-10-30)

Primary citation

Querol-Audi, J.,Konecsni, T.,Pous, J.,Carugo, O.,Fita, I.,Verdaguer, N.,Blaas, D.
Minor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition
Febs Lett., 583:235-240, 2009

PubMed Abstract: X-ray structures of human rhinovirus 2 (HRV2) in complex with soluble very-low-density lipoprotein receptors encompassing modules 1, 2, and 3 (V123) and five V3 modules arranged in tandem (V33333) demonstrates multi-modular binding around the virion's five-fold axes. Occupancy was 60% for V123 and 100% for V33333 explaining the high-avidity of the interaction. Surface potentials of 3D-models of all minor group HRVs and K-type major group HRVs were compared; hydrophobic interactions between a conserved lysine in the viruses and a tryptophan in the receptor modules together with coulombic attraction via diffuse opposite surface potentials determine minor group HRV receptor specificity.

PubMed: 19073182
DOI: 10.1016/j.febslet.2008.12.014

Experimental method

X-RAY DIFFRACTION (3.5 Å)