1D3L
D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES.
Summary for 1D3L
| Entry DOI | 10.2210/pdb1d3l/pdb |
| Descriptor | PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) (1 entity in total) |
| Functional Keywords | rhinovirus receptor, adhesion protein, glycoprotein, immunoglobulin fold, cell adhesion |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein: P05362 |
| Total number of polymer chains | 1 |
| Total formula weight | 20438.26 |
| Authors | Bella, J.,Kolatkar, P.R.,Rossmann, M.G. (deposition date: 1999-09-29, release date: 1999-12-01, Last modification date: 2023-08-09) |
| 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 Cited by 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: 10562537DOI: 10.1093/emboj/18.22.6249 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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