1ozn

<StructureSection load='1ozn' size='340' side='right' caption='[[1ozn]], [[Resolution|resolution]] 1.52&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ozn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OZN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OZN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTN4R OR NOGOR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ozn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ozn OCA], [http://pdbe.org/1ozn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ozn RCSB], [http://www.ebi.ac.uk/pdbsum/1ozn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ozn ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RTN4R_HUMAN RTN4R_HUMAN]] Receptor for RTN4, OMG and MAG. Mediates axonal growth inhibition and may play a role in regulating axonal regeneration and plasticity in the adult central nervous system. Acts in conjunction with RTN4 and LIGO1 in regulating neuronal precursor cell motility during cortical development (By similarity).<ref>PMID:12037567</ref> <ref>PMID:14966521</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12718853</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ozn" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Bazan, J F]]

[[Category: Garcia, K C]]

[[Category: He, X]]

[[Category: He, Z]]

[[Category: McDermott, G]]

[[Category: Park, J B]]

[[Category: Signaling protein]]