6IQG

X-ray crystal structure of Fc and peptide complex

Summary for 6IQG

• Entry DOI: 10.2210/pdb6iqg/pdb
• Descriptor: Immunoglobulin gamma-1 heavy chain, 18-mer peptide G(HCS)DCAYHRGELVWCT(HCS)H(NH2), 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, ... (5 entities in total)
• Functional Keywords: fc, complex, immune system
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 54504.43

Authors

Adachi, M.,Ito, Y. (deposition date: 2018-11-08, release date: 2019-02-13, Last modification date: 2024-11-13)

Primary citation

Kishimoto, S.,Nakashimada, Y.,Yokota, R.,Hatanaka, T.,Adachi, M.,Ito, Y.
Site-Specific Chemical Conjugation of Antibodies by Using Affinity Peptide for the Development of Therapeutic Antibody Format.
Bioconjug. Chem., 30:698-702, 2019

PubMed Abstract: Artificially modified IgG molecules are increasingly utilized in industrial and clinical applications. In the present study, the method of chemical conjugation by affinity peptide (CCAP) for site-specific chemical modification has been developed by using a peptide that bound with high affinity to human IgG-Fc. This method enabled a rapid modification of a specific residue (Lys248 on Fc) in a one-step reaction under mild condition to form a stable amide bond between the peptide and Fc. The monovalent peptide-IgG conjugate not only maintained complete antigen binding but also bound to Fc receptors (FcRn, FcγRI, and FcγRIIIa), indicating that it is a suitable conjugate form that can be further developed into highly functional antibody therapeutics. CCAP was applied for the preparation of an antibody-drug conjugate and a bispecific antibody to demonstrate the usefulness of this method.

PubMed: 30606013
DOI: 10.1021/acs.bioconjchem.8b00865

Experimental method

X-RAY DIFFRACTION (2.998 Å)