5amo

Structure of a mouse Olfactomedin-1 disulfide-linked dimer of the Olfactomedin domain and part of the coiled coil

spinqualitylabelsall models 5amo, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5amo is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CL, GOL, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NOE1_MOUSE May play an important role in regulating the production of neural crest cells by the neural tube. Publication Abstract from PubMed Olfactomedin-1 (Olfm1; also known as noelin, 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 determine 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 at the tips a C-terminal beta-propeller dimer. This agrees with our crystal structure of a C-terminal coiled-coil segment and beta-propeller combination (Olfm1coil-Olf), which reveals a disulfide-linked dimeric arrangement with the beta-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 informs on the conformation of several other olfactomedin domain family members. Olfactomedin-1 has a V-shaped disulfide-linked tetrameric structure.,Pronker MF, Bos TG, Sharp TH, Thies-Weesie DM, Janssen BJ J Biol Chem. 2015 Apr 21. pii: jbc.M115.653485. PMID:25903135 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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