1ozn
From Proteopedia
1.5A Crystal Structure of the Nogo Receptor Ligand Binding Domain Reveals a Convergent Recognition Scaffold Mediating Inhibition of Myelination
Overview
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.
About this Structure
1OZN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition., He XL, Bazan JF, McDermott G, Park JB, Wang K, Tessier-Lavigne M, He Z, Garcia KC, Neuron. 2003 Apr 24;38(2):177-85. PMID:12718853 Page seeded by OCA on Sat May 3 04:29:00 2008
Categories: Homo sapiens | Single protein | Bazan, J F. | Garcia, K C. | He, X. | He, Z. | McDermott, G. | Park, J B. | Crystal structure | Ligand binding | Mad | Mag | Myelination inhibition | Neuronal regeneration | Nogo receptor | Nogo-66 | Omgp | P75 | Signal transduction