1V9U

Human Rhinovirus 2 bound to a fragment of its cellular receptor protein

Summary for 1V9U

• Entry DOI: 10.2210/pdb1v9u/pdb
• Related: 1FPN
• Descriptor: Coat protein VP1, Coat protein VP2, Coat protein VP3, ... (7 entities in total)
• Functional Keywords: human rhinovirus, vldl-receptor, virus-protein complex, icosahedral virus, virus-receptor complex, virus/receptor
• Biological source: Homo sapiens (human); More
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P04936 P04936 P04936 P04936; Membrane; Single-pass type I membrane protein: P98155
• Total number of polymer chains: 5
• Total formula weight: 100172.38

Authors

Verdaguer, N.,Fita, I.,Reithmayer, M.,Moser, R.,Blaas, D. (deposition date: 2004-02-03, release date: 2004-05-04, Last modification date: 2024-10-09)

Primary citation

Verdaguer, N.,Fita, I.,Reithmayer, M.,Moser, R.,Blaas, D.
X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein
NAT.STRUCT.MOL.BIOL., 11:429-434, 2004

PubMed Abstract: Although many viral receptors have been identified, the ways in which they interact with their cognate viruses are not understood at the molecular level. We have determined the X-ray structure of a complex between calcium-containing modules of the very low-density lipoprotein receptor and the minor group human rhinovirus HRV2. The receptor binds close to the icosahedral five-fold vertex, with only one module per virus protomer. The binding face of this module is defined by acidic calcium-chelating residues and, in particular, by an exposed tryptophan that is highly conserved. The attachment site on the virus involves only residues from VP1, particularly a lysine strictly conserved in all minor group HRVs. The disposition of the attached ligand-binding repeats around the five-fold axis, together with the proximity of the N- and C-terminal ends of adjacent modules, suggests that more than one repeat in a single receptor molecule might attach simultaneously.

PubMed: 15064754
DOI: 10.1038/nsmb753

Experimental method

X-RAY DIFFRACTION (3.6 Å)