1ozn

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==Overview==
==Overview==
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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.
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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.
==Disease==
==Disease==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bazan, J.F.]]
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[[Category: Bazan, J F.]]
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[[Category: Garcia, K.C.]]
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[[Category: Garcia, K C.]]
[[Category: He, X.]]
[[Category: He, X.]]
[[Category: He, Z.]]
[[Category: He, Z.]]
[[Category: McDermott, G.]]
[[Category: McDermott, G.]]
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[[Category: Park, J.B.]]
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[[Category: Park, J B.]]
[[Category: ACY]]
[[Category: ACY]]
[[Category: crystal structure]]
[[Category: crystal structure]]
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[[Category: signal transduction]]
[[Category: signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:37:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:32 2008''

Revision as of 12:23, 21 February 2008


1ozn, resolution 1.52Å

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

Contents

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.

Disease

Known diseases associated with this structure: Schizophrenia, susceptibility to OMIM:[605566]

About this Structure

1OZN is a Single protein structure of sequence from Homo sapiens with as ligand. 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

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