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6WIB

Next generation monomeric IgG4 Fc

Summary for 6WIB
Entry DOI10.2210/pdb6wib/pdb
DescriptorImmunoglobulin heavy constant gamma 4, 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, ZINC ION, ... (4 entities in total)
Functional Keywordsantibody constant region, fragment crystallizable, mutated, immune system
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight25507.53
Authors
Oganesyan, V.Y.,Shan, L.,Dall'Acqua, W.,van Dyk, N. (deposition date: 2020-04-09, release date: 2021-09-15, Last modification date: 2024-11-13)
Primary citationShan, L.,Dyk, N.V.,Haskins, N.,Cook, K.M.,Rosenthal, K.L.,Mazor, R.,Dragulin-Otto, S.,Jiang, Y.,Wu, H.,Dall'Acqua, W.F.,Borrok, M.J.,Damschroder, M.M.,Oganesyan, V.
In vivo pharmacokinetic enhancement of monomeric Fc and monovalent bispecific designs through structural guidance.
Commun Biol, 4:1048-1048, 2021
Cited by
PubMed Abstract: In a biologic therapeutic landscape that requires versatility in targeting specificity, valency and half-life modulation, the monomeric Fc fusion platform holds exciting potential for the creation of a class of monovalent protein therapeutics that includes fusion proteins and bispecific targeting molecules. Here we report a structure-guided approach to engineer monomeric Fc molecules to adapt multiple versions of half-life extension modifications. Co-crystal structures of these monomeric Fc variants with Fc neonatal receptor (FcRn) shed light into the binding interactions that could serve as a guide for engineering the half-life of antibody Fc fragments. These engineered monomeric Fc molecules also enabled the generation of a novel monovalent bispecific molecular design, which translated the FcRn binding enhancement to improvement of in vivo serum half-life.
PubMed: 34497355
DOI: 10.1038/s42003-021-02565-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.55 Å)
Structure validation

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