6QHJ
High-resolution crystal structure of calcium- and sodium-bound mouse Olfactomedin-1 beta-propeller domain
Summary for 6QHJ
| Entry DOI | 10.2210/pdb6qhj/pdb |
| Descriptor | Noelin, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | calcium, beta-propeller, secreted, brain, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 31313.62 |
| Authors | Pronker, M.F.,van den Hoek, H.G.,Janssen, B.J.C. (deposition date: 2019-01-16, release date: 2019-09-11, Last modification date: 2024-11-20) |
| Primary citation | Pronker, M.F.,van den Hoek, H.,Janssen, B.J.C. Design and structural characterisation of olfactomedin-1 variants as tools for functional studies. BMC Mol Cell Biol, 20:50-50, 2019 Cited by PubMed Abstract: Olfactomedin-1 (Olfm1; also known as Noelin or Pancortin) is a highly-expressed secreted brain and retina protein and its four isoforms have different roles in nervous system development and function. Structural studies showed that the long Olfm1 isoform BMZ forms a disulfide-linked tetramer with a V-shaped architecture. The tips of the Olfm1 "V" each consist of two C-terminal β-propeller domains that enclose a calcium binding site. Functional characterisation of Olfm1 may be aided by new biochemical tools derived from these core structural elements. PubMed: 31726976DOI: 10.1186/s12860-019-0232-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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