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TitleConformational Changes in Ige Contribute to its Uniquely Slow Dissociation Rate from Receptor Fceri
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 18, Page 571-, Year 2011
Publish dateAug 26, 2009 (structure data deposition date)
AuthorsHoldom, M.D. / Davies, A.M. / Nettleship, J.E. / Bagby, S.C. / Dhaliwal, B. / Girardi, E. / Hunt, J. / Gould, H.J. / Beavil, A.J. / Mcdonnell, J.M. ...Holdom, M.D. / Davies, A.M. / Nettleship, J.E. / Bagby, S.C. / Dhaliwal, B. / Girardi, E. / Hunt, J. / Gould, H.J. / Beavil, A.J. / Mcdonnell, J.M. / Owens, R.J. / Sutton, B.J.
External linksNat. Struct. Mol. Biol. / PubMed:21516097
MethodsX-ray diffraction
Resolution1.9 - 3.4 Å
Structure data

PDB-2wqr:
The high resolution crystal structure of IgE Fc
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2y7q:
THE HIGH-AFFINITY COMPLEX BETWEEN IGE AND ITS RECEPTOR FC EPSILON RI
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

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

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / IMMUNOGLOBULIN DOMAIN / GLYCOPROTEIN / ALLERGY / ANTIBODY / IGE-BINDING PROTEIN / HIGH-AFFINITY RECEPTOR / IMMUNOGLOBULIN C REGION

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