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Domain Metastability: A Molecular Basis for Immunoglobulin Deposition?

DOI: 10.1016/j.jmb.2010.04.011 DOI Help

Authors: Andreas F.-p. Sonnen (University of Oxford) , Chao Yu (University of Oxford) , Edward J. Evans (University of Oxford) , David I. Stuart (The Wellcome Trust Centre for Human Genetics, University of Oxford) , Simon J. Davies (University of Oxford) , Robert J. C. Gilbert (The Wellcome Trust Centre for Human Genetics, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Molecular Biology , VOL 399 (2) , PAGES 207-213

State: Published (Approved)
Published: June 2010

Abstract: We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis–trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand swapping. Our results suggest a molecular basis for the pathological aggregation of immunoglobulin domains and why amyloid-like fibres are more often composed of homologous rather than heterologous subunits.

Journal Keywords: Ctla-4; X-Ray Crystallography; Protein Aggregation Assays; Electron Microscopy; Amyloid

Subject Areas: Biology and Bio-materials


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