English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity

MPS-Authors
/persons/resource/persons217811

Li,  Aitao
Department of Chemistry, Philipps-Universität Marburg;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

/persons/resource/persons58919

Reetz,  Manfred T.
Department of Chemistry, Philipps-Universität Marburg;
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Schrimpf, A., Hempel, F., Li, A., Linne, U., Maier, U. G., Reetz, M. T., et al. (2018). Hinge-Type Dimerization of Proteins by a Tetracysteine Peptide of High Pairing Specificity. Biochemistry, 57(26), 3658-3664. doi:10.1021/acs.biochem.8b00475.


Cite as: https://hdl.handle.net/21.11116/0000-0001-EC55-6
Abstract
Dimeric disulfide-linked peptides are formed by the regioselective oxidative folding of thiol precursors containing the CX3CX2CX3C tetracysteine motif. Here, we investigate the general applicability of this peptide as a dimerization motif for different proteins. By recombinant DNA technology, the peptide CHWECRGCRLVC was loaded with proteins, and functional homodimers were obtained upon oxidative folding. Attached to the N-terminus of the dodecapeptide, the prokaryotic enzyme limonene epoxide hydrolase (LEH) completely forms a covalent antiparallel dimer. In a diatom expression system, the monoclonal antibody CL4 mAb is released in its functional form when its natural CPPC central parallel hinge is exchanged for the designed tetra-Cys hinge motif. To improve our understanding of the regioselectivity of tetra-disulfide formation, we provoked the formation of heterodimeric hinge peptides by mixing two different tetra-Cys peptides and characterizing the heterodimer by mass spectrometry and nuclear magnetic resonance spectroscopy.