1XPH
Structure of DC-SIGNR and a portion of repeat domain 8
Summary for 1XPH
| Entry DOI | 10.2210/pdb1xph/pdb |
| Descriptor | CD209 antigen-like protein 1, CALCIUM ION (3 entities in total) |
| Functional Keywords | c-type lectin, carbohydrate recognition domain, repeat domain, immune system, sugar binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Cell membrane; Single-pass type II membrane protein (Potential). Isoform 2: Cell membrane; Single-pass type II membrane protein (Potential). Isoform 3: Cell membrane; Single-pass type II membrane protein (Potential). Isoform 5: Secreted (Potential). Isoform 6: Secreted (Potential). Isoform 7: Secreted (Potential). Isoform 10: Secreted (Potential): Q9H2X3 |
| Total number of polymer chains | 1 |
| Total formula weight | 17603.30 |
| Authors | Snyder, G.A.,Colonna, M.,Sun, P.D. (deposition date: 2004-10-08, release date: 2005-04-19, Last modification date: 2024-11-13) |
| Primary citation | Snyder, G.A.,Colonna, M.,Sun, P.D. The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer. J.Mol.Biol., 347:979-989, 2005 Cited by PubMed Abstract: The dendritic cell-specific ICAM-3 non-integrin (DC-SIGN) and its close relative DC-SIGNR recognize various glycoproteins, both pathogenic and cellular, through the receptor lectin domain-mediated carbohydrate recognition. While the carbohydrate-recognition domains (CRD) exist as monomers and bind individual carbohydrates with low affinity and are permissive in nature, the full-length receptors form tetramers through their repeat domain and recognize specific ligands with high affinity. To understand the tetramer-based ligand binding avidity, we determined the crystal structure of DC-SIGNR with its last repeat region. Compared to the carbohydrate-bound CRD structure, the structure revealed conformational changes in the calcium and carbohydrate coordination loops of CRD, an additional disulfide bond between the N and the C termini of the CRD, and a helical conformation for the last repeat. On the basis of the current crystal structure and other published structures with sequence homology to the repeat domain, we generated a tetramer model for DC-SIGN/R using homology modeling and propose a ligand-recognition index to identify potential receptor ligands. PubMed: 15784257DOI: 10.1016/j.jmb.2005.01.063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.41 Å) |
Structure validation
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