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Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains

Georg J. Rottenaicher, Benedikt Weber, Florian Rührnößl, Pamina Kazman, Ramona M. Absmeier, Manuel Hitzenberger, Martin Zacharias, Johannes Büchner

2021Journal of Biological Chemistry47 citationsDOIOpen Access PDF

Abstract

domain in a specific way, increasing the dynamics of framework regions, which can then change their conformation to form the fibril core. These findings reveal unexpected influences of CDR-framework interactions on antibody architecture, stability, and amyloid propensity.

Topics & Concepts

Hypervariable regionImmunoglobulin light chainMechanism (biology)AntibodyChemistryMutationGeneticsBiologyBiophysicsMolecular biologyBiochemistryGenePhysicsQuantum mechanicsMonoclonal and Polyclonal Antibodies ResearchAmyloidosis: Diagnosis, Treatment, OutcomesProtein purification and stability
Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains | Litcius