Crystal structure of the Nogo-Receptor-2 Journal Article


Authors: Semavina, M.; Saha, N.; Kolev, M. V.; Goldgur, Y.; Giger, R. J.; Himanen, J. P.; Nikolov, D. B.
Article Title: Crystal structure of the Nogo-Receptor-2
Abstract: 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. © 2011 The Protein Society.
Keywords: unclassified drug; binding affinity; protein domain; protein binding; protein purification; glycosylation; crystal structure; protein structure; x ray crystallography; ligand binding; x-ray crystallography; nogo receptor; nogo receptor 1; nogo receptor 2; protein nogo
Journal Title: Protein Science
Volume: 20
Issue: 4
ISSN: 0961-8368
Publisher: Wiley Blackwell  
Date Published: 2011-04-01
Start Page: 684
End Page: 689
Language: English
DOI: 10.1002/pro.597
PROVIDER: scopus
PUBMED: 21308849
PMCID: PMC3081546
DOI/URL:
Notes: --- - "Export Date: 23 June 2011" - "CODEN: PRCIE" - "Source: Scopus"
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MSK Authors
  1. Dimitar B Nikolov
    86 Nikolov
  2. Juha P Himanen
    50 Himanen
  3. Yehuda Goldgur
    42 Goldgur
  4. Nayanendu Saha
    23 Saha
  5. Momchil V Kolev
    7 Kolev