5AMO
Structure of a mouse Olfactomedin-1 disulfide-linked dimer of the Olfactomedin domain and part of the coiled coil
Summary for 5AMO
| Entry DOI | 10.2210/pdb5amo/pdb |
| Descriptor | NOELIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | signaling protein, olfm1, disulfide, neurobiology, development, ampa receptor, beta propeller |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) |
| Total number of polymer chains | 2 |
| Total formula weight | 110603.00 |
| Authors | Pronker, M.F.,Bos, T.G.A.A.,Sharp, T.H.,Thies-Weesie, D.M.,Janssen, B.J.C. (deposition date: 2015-03-11, release date: 2015-04-29, Last modification date: 2024-11-13) |
| Primary citation | Pronker, M.F.,Bos, T.G.A.A.,Sharp, T.H.,Thies-Weesie, D.M.,Janssen, B.J.C. Olfactomedin-1 Has a V-Shaped Disulfide-Linked Tetrameric Structure. J.Biol.Chem., 290:15092-, 2015 Cited by PubMed Abstract: Olfactomedin-1 (Olfm1; also known as noelin and pancortin) is a member of the olfactomedin domain-containing superfamily and a highly expressed neuronal glycoprotein important for nervous system development. It binds a number of secreted proteins and cell surface-bound receptors to induce cell signaling processes. Using a combined approach of x-ray crystallography, solution scattering, analytical ultracentrifugation, and electron microscopy we determined that full-length Olfm1 forms disulfide-linked tetramers with a distinctive V-shaped architecture. The base of the "V" is formed by two disulfide-linked dimeric N-terminal domains. Each of the two V legs consists of a parallel dimeric disulfide-linked coiled coil with a C-terminal β-propeller dimer at the tips. This agrees with our crystal structure of a C-terminal coiled-coil segment and β-propeller combination (Olfm1(coil-Olf)) that reveals a disulfide-linked dimeric arrangement with the β-propeller top faces in an outward exposed orientation. Similar to its family member myocilin, Olfm1 is stabilized by calcium. The dimer-of-dimers architecture suggests a role for Olfm1 in clustering receptors to regulate signaling and sheds light on the conformation of several other olfactomedin domain family members. PubMed: 25903135DOI: 10.1074/JBC.M115.653485 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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