Biological and structural characterization of glycosylation on ephrin-a1, a preferred ligand for EPHA2 receptor tyrosine kinase Journal Article

   


Authors: Ferluga, S.; Hantgan, R.; Goldgur, Y.; Himanen, J. P.; Nikolov, D. B.; Debinski, W.
Article Title: Biological and structural characterization of glycosylation on ephrin-a1, a preferred ligand for EPHA2 receptor tyrosine kinase
Abstract: Background: Ephrin-A1 is the preferred ligand for EphA2 receptor. Results: Biological assays and crystal structure analysis document that ephrin-A1 deglycosylation abrogates ligand's binding and receptor activation, and also protein folding and cellular localization. Conclusion: The glycosylation of ephrin-A1 enables EphA2 receptor binding and activation by stabilizing Eph/ephrin heterotetramers. Significance: The glycosylation of ephrin-A1 is indispensable for the protein biological activity. © 2013 by The American Society.
Journal Title: Journal of Biological Chemistry
Volume: 288
Issue: 25
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 2013-06-21
Start Page: 18448
End Page: 18457
Language: English
DOI: 10.1074/jbc.M113.464008
PROVIDER: scopus
PMCID: PMC3689987
PUBMED: 23661698
DOI/URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-84880077063&partnerID=40&md5=0212501fb674dbda5c3531f3db0ba7b6
Notes: --- - "Export Date: 1 August 2013" - "CODEN: JBCHA" - "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
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