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Article

Solution conformation of wild-type and mutant IgG3 and IgG4 immunoglobulins using crystallohydrodynamics: possible implications for complement activation.

Biophysical journal - 1 Dec 2007

Lu Yanling, Harding Stephen E, Michaelsen Terje E, Longman Emma, Davis Kenneth G, Ortega Alvaro, Grossmann J Günter, Sandlie Inger, García de la Torre José

Abstract excerpt

We have employed the recently described crystallohydrodynamic approach to compare the time-averaged domain orientation of human chimeric IgG3wt (wild-type) and IgG4wt as well as two hinge mutants of IgG3 and an IgG4S331P (mutation from serine to proline at position 331, EU numbering) mutant of IgG4. The approach involves combination of the known shape of the Fab and Fc regions from crystallography with...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17704171
DOI: 10.1529/biophysj.107.108993
PMCID: PMC2084252

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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