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2Y7Q

THE HIGH-AFFINITY COMPLEX BETWEEN IGE AND ITS RECEPTOR FC EPSILON RI

Summary for 2Y7Q
Entry DOI10.2210/pdb2y7q/pdb
Related1F2Q 1F6A 1FP5 1G84 1IGE 1J86 1J87 1J88 1J89 1O0V 1RPQ
DescriptorHIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR SUBUNIT ALPHA, IG EPSILON CHAIN C REGION, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsallergy, antibody, ige-binding protein, high-affinity receptor, immunoglobulin c region, immune system
Biological sourceHOMO SAPIENS (HUMAN)
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Total number of polymer chains3
Total formula weight95843.97
Authors
Davies, A.M.,Holdom, M.D.,Nettleship, J.E.,Beavil, A.J.,Owens, R.J.,Sutton, B.J. (deposition date: 2011-02-01, release date: 2011-04-20, Last modification date: 2023-12-20)
Primary citationHoldom, 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.
Conformational Changes in Ige Contribute to its Uniquely Slow Dissociation Rate from Receptor Fceri
Nat.Struct.Mol.Biol., 18:571-, 2011
Cited by
PubMed: 21516097
DOI: 10.1038/NSMB.2044
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.4 Å)
Structure validation

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