4d7c

Monoclinic crystal form of the extracellular olfactomedin domain from gliomedin

spinqualitylabelsall models 4d7c, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d7c is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA Related: 4d77 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed All members of the olfactomedin (OLF) family have a conserved extracellular OLF domain, for which a structure has not been available. We present here the crystal structure of the OLF domain from gliomedin. Gliomedin is a protein expressed by Schwann cells in peripheral nerves, important for the formation of the nodes of Ranvier. Gliomedin interacts with neuronal cell adhesion molecules, such as neurofascin, but the structural details of the interaction are not known. The structure of the OLF domain presents a 5-bladed beta-propeller fold, with unusual geometric properties. The symmetry of the structure is not 5-fold, but rather, reveals a twisted arrangement. The conserved top face of the gliomedin OLF domain is likely to be important for binding to neuronal ligands. Our results provide a structural basis for the functions of gliomedin in Schwann cells, enable the understanding of the role of the gliomedin OLF domain in autoimmune neuropathies, and unravel the locations of human disease-causing mutations in other OLF family members, including myocilin. The Olfactomedin Domain from Gliomedin is a beta-Propeller with Unique Structural Properties.,Han H, Kursula P J Biol Chem. 2014 Dec 17. pii: jbc.M114.627547. PMID:25525261 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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