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TitleStructural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor.
Journal, issue, pagesEMBO J, Vol. 18, Issue 22, Page 6249-6259, Year 1999
Publish dateNov 15, 1999
AuthorsP R Kolatkar / J Bella / N H Olson / C M Bator / T S Baker / M G Rossmann /
PubMed AbstractTwo 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 ...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.
External linksEMBO J / PubMed:10562537 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.25 - 28 Å
Structure data

PDB-1d3e:
CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) 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
Method: ELECTRON MICROSCOPY / Resolution: 28.0 Å

PDB-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
Method: ELECTRON MICROSCOPY / Resolution: 26.0 Å

PDB-1d3l:
D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES.
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

Source
  • homo sapiens (human)
  • human rhinovirus sp.
KeywordsVirus/Receptor / HUMAN RHINOVIRUS / HRV16 / 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 / HRV14 / CELL ADHESION / RHINOVIRUS RECEPTOR / ADHESION PROTEIN / GLYCOPROTEIN / IMMUNOGLOBULIN FOLD

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