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Structure paper

TitleResolution of disulfide heterogeneity in Nogo receptor 1 fusion proteins by molecular engineering.
Journal, issue, pagesBiotechnol Appl Biochem, Vol. 57, Page 31-45, Year 2010
Publish dateNov 2, 2009 (structure data deposition date)
AuthorsWeinreb, P.H. / Wen, D. / Qian, F. / Wildes, C.P. / Garber, E.A. / Walus, L. / Jung, M.Y. / Wang, J. / Relton, J.K. / Amatucci, J. ...Weinreb, P.H. / Wen, D. / Qian, F. / Wildes, C.P. / Garber, E.A. / Walus, L. / Jung, M.Y. / Wang, J. / Relton, J.K. / Amatucci, J. / Wang, R. / Porreca, F. / Silvian, L. / Meier, W. / Pepinsky, R.B. / Lee, D.H.
External linksBiotechnol Appl Biochem / PubMed:20815818
MethodsX-ray diffraction
Resolution3.1 Å
Structure data

PDB-3kj4:
Structure of rat Nogo receptor bound to 1D9 antagonist antibody
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-ZN:
Unknown entry

ChemComp-NDG:
2-acetamido-2-deoxy-alpha-D-glucopyranose

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • mus musculus (house mouse)
  • rattus norvegicus (Norway rat)
KeywordsIMMUNE SYSTEM / Nogo receptor antagonist antibody / LRR / Cell membrane / Disulfide bond / Glycoprotein / GPI-anchor / Leucine-rich repeat / Lipoprotein / Membrane / Receptor

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