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Article

Mutations within a human IgG2 antibody form distinct and homogeneous disulfide isomers but do not affect Fc gamma receptor or C1q binding.

Protein science : a publication of the Protein Society - 1 Apr 2010

Lightle Sandra, Aykent Serdar, Lacher Nathan, Mitaksov Vesselin, Wells Kristine, Zobel James, Oliphant Theodore

Abstract excerpt

Human IgG2 antibodies may exist in at least three distinct structural isomers due to disulfide shuffling within the upper hinge region. Antibody interactions with Fc gamma receptors and the complement component C1q contribute to immune effector functions. These interactions could be impacted by the accessibility and structure of the hinge region. To examine the role structural isomers may have on effector...

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Identifiers

PMID: 20120022
DOI: 10.1002/pro.352
PMCID: PMC2867015

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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