1D3I

CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY

Summary for 1D3I

• Entry DOI: 10.2210/pdb1d3i/pdb
• Descriptor: PROTEIN (INTERCELLULAR ADHESION MOLECULE-1), PROTEIN (RHINOVIRUS 14 COAT PROTEIN VP1), PROTEIN (RHINOVIRUS 14 COAT PROTEIN VP2), ... (5 entities in total)
• Functional Keywords: human rhinovirus, hrv14, icam-1, fitting of x-ray structures into cryo-em reconstructions, common cold, virus uncoating, virus/ viral protein, rhinovirus-receptor complex, icosahedral virus, virus-receptor complex, virus/receptor
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 114920.79

Authors

Bella, J.,Rossmann, M.G. (deposition date: 1999-09-29, release date: 2000-01-19, Last modification date: 2024-04-17)

Primary citation

Kolatkar, P.R.,Bella, J.,Olson, N.H.,Bator, C.M.,Baker, T.S.,Rossmann, M.G.
Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor.
EMBO J., 18:6249-6259, 1999

PubMed Abstract: Two human rhinovirus serotypes complexed with two- and five-domain soluble fragments of the cellular receptor, intercellular adhesion molecule-1, have been investigated by X-ray crystallographic analyses of the individual components and by cryo-electron microscopy of the complexes. The three-dimensional image reconstructions provide a molecular envelope within which the crystal structures of the viruses and the receptor fragments can be positioned with accuracy. The N-terminal domain of the receptor binds to the rhinovirus 'canyon' surrounding the icosahedral 5-fold axes. Fitting of molecular models into the image reconstruction density identified the residues on the virus that interact with those on the receptor surface, demonstrating complementarity of the electrostatic patterns for the tip of the N-terminal receptor domain and the floor of the canyon. The complexes seen in the image reconstructions probably represent the first stage of a multistep binding process. A mechanism is proposed for the subsequent viral uncoating process.

PubMed: 10562537
DOI: 10.1093/emboj/18.22.6249

Experimental method

ELECTRON MICROSCOPY (26 Å)