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Heuristic models of the intermonomeric disulfide bonding process
D A Evans1, J Klemer, S L Kaattari
1Department of Physical Sciences, Virginia Institute of Marine Science/School of Marine Science, College of William and Mary, Gloucester Point, VA 23062 1346, USA.
Journal of Theoretical Biology
|December 5, 1998
Summary
Researchers modeled trout Immunoglobulin M (IgM) assembly, suggesting disulfide bond formation occurs late in secretion. This process may accelerate with existing bonds, impacting tetramer structure.
Area of Science:
- Immunology
- Biochemistry
- Structural Biology
Background:
- Immunoglobulin M (IgM) is a crucial antibody with a complex quaternary structure.
- Understanding the assembly of disulfide-bonded IgM is vital for immunology and protein folding studies.
Purpose of the Study:
- To model the heuristic assembly of fully disulfide-bonded trout Immunoglobulin M (IgM).
- To investigate the sequential formation of disulfide bonds (DSB) during IgM assembly.
- To compare model predictions with experimentally observed subunit ratios.
Main Methods:
- Heuristic modeling of sequential disulfide bond formation.
- Focus on bond formation rates rather than biochemical mechanisms.
- Comparison of predicted and experimental ratios of covalently-linked subunits.
Main Results:
- The final stages of trout IgM assembly, involving disulfide bond formation, likely occur late in the secretory pathway.
- Incompletely crosslinked tetramers are a probable outcome of this late-stage assembly.
- The rate of disulfide bond formation within a tetramer may increase with previously formed inter-monomeric DSBs.
Conclusions:
- Trout IgM assembly involves sequential disulfide bond formation, predominantly late in the secretory process.
- The presence of existing disulfide bonds can accelerate further bond formation within the tetramer.
- These findings offer insights into the structural assembly and maturation of IgM antibodies.