1OZN
1.5A Crystal Structure of the Nogo Receptor Ligand Binding Domain Reveals a Convergent Recognition Scaffold Mediating Inhibition of Myelination
Summary for 1OZN
| Entry DOI | 10.2210/pdb1ozn/pdb |
| Descriptor | Reticulon 4 receptor, alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | nogo receptor, mad, myelination inhibition, omgp, mag, nogo-66, p75, signal transduction, neuronal regeneration, ligand binding, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Lipid-anchor, GPI-anchor: Q9BZR6 |
| Total number of polymer chains | 1 |
| Total formula weight | 33128.76 |
| Authors | He, X.,Bazan, J.F.,Park, J.B.,McDermott, G.,He, Z.,Garcia, K.C. (deposition date: 2003-04-09, release date: 2003-05-20, Last modification date: 2024-11-20) |
| Primary citation | He, X.L.,Bazan, J.F.,McDermott, G.,Park, J.B.,Wang, K.,Tessier-Lavigne, M.,He, Z.,Garcia, K.C. Structure of the Nogo Receptor Ectodomain. A Recognition module implicated in Myelin Inhibition. Neuron, 38:177-185, 2003 Cited by PubMed Abstract: Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin. Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands. Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor. Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites. A deep cleft at the C-terminal base of the LRR may play a role in NgR association with the p75 coreceptor. These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition. PubMed: 12718853DOI: 10.1016/S0896-6273(03)00232-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.52 Å) |
Structure validation
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