4p91

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'''Unreleased structure'''
 
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The entry 4p91 is ON HOLD
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==Crystal structure of the nogo-receptor-2 (27-330)==
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<StructureSection load='4p91' size='340' side='right'caption='[[4p91]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4p91]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P91 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4p91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p91 OCA], [https://pdbe.org/4p91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p91 RCSB], [https://www.ebi.ac.uk/pdbsum/4p91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p91 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/R4RL2_RAT R4RL2_RAT]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Semavina, M., Saha, N., Kolev, M., Goldgur, Y., Giger, R., Himanen, J., Nikolov, D.
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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>
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Description: Crystal structure of the nogo-receptor-2 (27-330)
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4p91" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
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[[Category: Giger R]]
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[[Category: Goldgur Y]]
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[[Category: Himanen J]]
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[[Category: Kolev M]]
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[[Category: Nikolov D]]
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[[Category: Saha N]]
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[[Category: Semavina M]]

Current revision

Crystal structure of the nogo-receptor-2 (27-330)

PDB ID 4p91

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