5FFL
Crystal structure of mouse CD300lf at 1.6 Angstroms resolution.
Summary for 5FFL
| Entry DOI | 10.2210/pdb5ffl/pdb |
| Descriptor | CD300 antigen-like family member F, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | cd300lf, cd300f, clm-1, clm1, irem-1, irem1, igsf13, lmir3, nkir, inhibitory receptor, ig superfamily, cd300 molecule-like family member f, immunoglobulin superfamily member, cell surface receptor, immune system |
| Biological source | Mus musculus |
| Cellular location | Cell membrane ; Single-pass type I membrane protein : Q6SJQ7 |
| Total number of polymer chains | 1 |
| Total formula weight | 13284.13 |
| Authors | Nelson, C.A.,Fremont, D.H. (deposition date: 2015-12-18, release date: 2016-08-31, Last modification date: 2024-11-13) |
| Primary citation | Orchard, R.C.,Wilen, C.B.,Doench, J.G.,Baldridge, M.T.,McCune, B.T.,Lee, Y.C.,Lee, S.,Pruett-Miller, S.M.,Nelson, C.A.,Fremont, D.H.,Virgin, H.W. Discovery of a proteinaceous cellular receptor for a norovirus. Science, 353:933-936, 2016 Cited by PubMed Abstract: Noroviruses (NoVs) are a leading cause of gastroenteritis globally, yet the host factors required for NoV infection are poorly understood. We identified host molecules that are essential for murine NoV (MNoV)-induced cell death, including CD300lf as a proteinaceous receptor. We found that CD300lf is essential for MNoV binding and replication in cell lines and primary cells. Additionally, Cd300lf(-/-) mice are resistant to MNoV infection. Expression of CD300lf in human cells breaks the species barrier that would otherwise restrict MNoV replication. The crystal structure of the CD300lf ectodomain reveals a potential ligand-binding cleft composed of residues that are critical for MNoV infection. Therefore, the presence of a proteinaceous receptor is the primary determinant of MNoV species tropism, whereas other components of cellular machinery required for NoV replication are conserved between humans and mice. PubMed: 27540007DOI: 10.1126/science.aaf1220 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.602 Å) |
Structure validation
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