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1I1C

NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A

Summary for 1I1C
Entry DOI10.2210/pdb1i1c/pdb
Related1I1A 1fc1
DescriptorIG GAMMA-2A CHAIN C REGION, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordsigg, fc, immune system
Biological sourceRattus norvegicus (Norway rat)
Total number of polymer chains2
Total formula weight56228.41
Authors
Martin, W.L.,West Jr., A.P.,Gan, L.,Bjorkman, P.J. (deposition date: 2001-01-31, release date: 2001-02-14, Last modification date: 2024-11-13)
Primary citationMartin, W.L.,West Jr., A.P.,Gan, L.,Bjorkman, P.J.
Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding.
Mol.Cell, 7:867-877, 2001
Cited by
PubMed Abstract: The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across epithelia, binding IgG in acidic vesicles (pH < or = 6.5) and releasing IgG in the blood at pH 7.4. Well-ordered FcRn/Fc crystals are prevented by the formation of "oligomeric ribbons" of FcRn dimers bridged by Fc homodimers, thus we crystallized a 1:1 complex between rat FcRn and a heterodimeric Fc containing only one FcRn binding site. The 2.8 A complex structure demonstrates that FcRn uses its alpha2 and beta2-microglobulin domains and carbohydrate to interact with the Fc C(gamma)2-C(gamma)3 interface. The structure reveals conformational changes in Fc and three titratable salt bridges that confer pH-dependent binding, and can be used to guide rational design of therapeutic IgGs with longer serum half-lives.
PubMed: 11336709
DOI: 10.1016/S1097-2765(01)00230-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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