4p8s
From Proteopedia
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| - | + | ==Crystal structure of Nogo-receptor-2== | |
| - | === | + | <StructureSection load='4p8s' size='340' side='right' caption='[[4p8s]], [[Resolution|resolution]] 1.80Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4p8s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P8S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P8S FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ozn|1ozn]], [[4p91|4p91]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rtn4rl2, Ngrh1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p8s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p8s RCSB], [http://www.ebi.ac.uk/pdbsum/4p8s PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The inhibition of axon regeneration upon mechanical injury is dependent on interactions between Nogo receptors (NgRs) and their myelin-derived ligands. NgRs are composed of a leucine-rich repeat (LRR) region, thought to be structurally similar among the different isoforms of the receptor, and a divergent "stalk" region. It has been shown by others that the LRR and stalk regions of NgR1 and NgR2 have distinct roles in conferring binding affinity to the myelin associated glycoprotein (MAG) in vivo. Here, we show that purified recombinant full length NgR1 and NgR2 maintain significantly higher binding affinity for purified MAG as compared to the isolated LRR region of either NgR1 or NgR2. We also present the crystal structure of the LRR and part of the stalk regions of NgR2 and compare it to the previously reported NgR1 structure with respect to the distinct signaling properties of the two receptor isoforms. | ||
| - | + | Crystal structure of the Nogo-receptor-2.,Semavina M, Saha N, Kolev MV, Goldgur Y, Giger RJ, Himanen JP, Nikolov DB Protein Sci. 2011 Apr;20(4):684-9. doi: 10.1002/pro.597. PMID:21308849<ref>PMID:21308849</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Buffalo rat]] | ||
[[Category: Giger, R J.]] | [[Category: Giger, R J.]] | ||
[[Category: Himanen, J P.]] | [[Category: Himanen, J P.]] | ||
Revision as of 06:44, 11 June 2014
Crystal structure of Nogo-receptor-2
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