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3dpr
From Proteopedia
| 3dpr, resolution 3.50Å () | |
|---|---|
| Sites: | and |
| Ligands: | , |
| Domains: | Pico_P1A, rhv |
| Resources: | FirstGlance, OCA, PDBsum, RCSB |
| Coordinates: | save as pdb, mmCIF, xml |
Human rhinovirus 2 bound to a concatamer of the VLDL receptor module V3
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.
Minor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognition., Querol-Audi J, Konecsni T, Pous J, Carugo O, Fita I, Verdaguer N, Blaas D, FEBS Lett. 2009 Jan 5;583(1):235-40. Epub 2008 Dec 13. PMID:19073182
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3DPR is a 5 chains structure of sequences from Homo sapiens and Human rhinovirus 2. Full crystallographic information is available from OCA.
Reference
- 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. 2009 Jan 5;583(1):235-40. Epub 2008 Dec 13. PMID:19073182 doi:10.1016/j.febslet.2008.12.014
Page seeded by OCA on Wed May 6 10:50:38 2009
Categories: Homo sapiens | Human rhinovirus 2 | Fita, I. | Pous, J. | Querol-Audi, J. | Verdaguer, N. | Alternative splicing | Atp-binding | Capsid protein | Cholesterol metabolism | Coated pit | Covalent protein-rna linkage | Cytoplasm | Cytoplasmic vesicle | Egf-like domain | Endocytosis | Glycoprotein | Helicase | Host-virus interaction | Human rhinovirus | Hydrolase | Icosahedral virus | Lipid metabolism | Lipid transport | Lipoprotein | Membrane | Myristate | Nucleotide-binding | Nucleotidyltransferase | Phosphoprotein | Polymorphism | Protease | Receptor | Rna replication | Rna-binding | Rna-directed rna polymerase | Steroid metabolism | Thiol protease | Transferase | Transmembrane | Transport | Virion | Virus-protein complex | Vldl | Vldl-receptor
