PDBsum entry 6iqh

Immune system

PDB id: 6iqh

Contents

Protein chains

207 a.a.

13 a.a.

Ligands

NAG-NAG-BMA-MAN-NAG-MAN-NAG-FUC ×2

GUA ×2

PDB id:

6iqh

Name:

Immune system

Title:

X-ray crystal structure of covalent-bonded complex of fc and peptide

Structure:

Immunoglobulin gamma-1 heavy chain. Chain: a, b. Synonym: immunoglobulin gamma-1 heavy chain nie. Engineered: yes. 17-mer peptide (gpdcayhkgelvwctfh). Chain: c, d. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Synthetic: yes. Synthetic construct. Organism_taxid: 32630

Resolution:

3.00Å R-factor: 0.227 R-free: 0.293

Authors:

M.Adachi,Y.Ito

Key ref:

S.Kishimoto et al. (2019). Site-Specific Chemical Conjugation of Antibodies by Using Affinity Peptide for the Development of Therapeutic Antibody Format. Bioconjug Chem, 30, 698-702. PubMed id: 30606013 DOI: 10.1021/acs.bioconjchem.8b00865

Date:

08-Nov-18 Release date: 13-Feb-19

Protein chains

P0DOX5  (IGG1_HUMAN) -  Immunoglobulin gamma-1 heavy chain from Homo sapiens

Seq: 449 a.a.

Struc: 207 a.a.

Protein chains

No UniProt id for this chain

Struc: 13 a.a.

DOI no: 10.1021/acs.bioconjchem.8b00865

Bioconjug Chem 30:698-702 (2019)

PubMed id: 30606013

Site-Specific Chemical Conjugation of Antibodies by Using Affinity Peptide for the Development of Therapeutic Antibody Format.

S.Kishimoto, Y.Nakashimada, R.Yokota, T.Hatanaka, M.Adachi, Y.Ito.

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.