1I1C
NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A
Summary for 1I1C
Entry DOI | 10.2210/pdb1i1c/pdb |
Related | 1I1A 1fc1 |
Descriptor | IG 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 Keywords | igg, fc, immune system |
Biological source | Rattus norvegicus (Norway rat) |
Total number of polymer chains | 2 |
Total formula weight | 56228.41 |
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 citation | Martin, 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: 11336709DOI: 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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