1OZN

1.5A Crystal Structure of the Nogo Receptor Ligand Binding Domain Reveals a Convergent Recognition Scaffold Mediating Inhibition of Myelination

1OZN の概要

• エントリーDOI: 10.2210/pdb1ozn/pdb
• 分子名称: 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)
• 機能のキーワード: nogo receptor, mad, myelination inhibition, omgp, mag, nogo-66, p75, signal transduction, neuronal regeneration, ligand binding, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor: Q9BZR6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33128.76

構造登録者

He, X.,Bazan, J.F.,Park, J.B.,McDermott, G.,He, Z.,Garcia, K.C. (登録日: 2003-04-09, 公開日: 2003-05-20, 最終更新日: 2024-11-20)

主引用文献

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

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: 12718853
DOI: 10.1016/S0896-6273(03)00232-0

実験手法

X-RAY DIFFRACTION (1.52 Å)