To the top

Page Manager: Webmaster
Last update: 9/11/2012 3:13 PM

Tell a friend about this page
Print version

Function of the CysD doma… - University of Gothenburg, Sweden Till startsida
To content Read more about how we use cookies on

Function of the CysD domain of the gel-forming MUC2 mucin.

Journal article
Authors Daniel Ambort
Sjoerd van der Post
Malin E V Johansson
J. Mackenzie
Elisabeth Thomsson
Ute Krengel
Gunnar C. Hansson
Published in Biochem Journal
Volume 436
Pages 61-70
Publication year 2011
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 61-70
Language en
Subject categories Basic Medicine


The colonic human MUC2 mucin forms a polymeric gel by covalent disulfide bonds in its N- and C-termini. The middle part of MUC2 is largely composed of two highly O-glycosylated mucin domains that are interrupted by a CysD domain of unknown function. We studied its function as recombinant proteins fused to a removable immunoglobulin Fc domain. Analysis of affinity-purified fusion proteins by native gel electrophoresis and gel filtration showed that they formed oligomeric complexes. Analysis of the individual isolated CysD parts showed that they formed dimers both when flanked by two MUC2 tandem repeats and without these. Cleavages of the two non-reduced CysD fusion proteins and analysis by MS revealed the localization of all five CysD disulfide bonds and that the predicted C-mannosylated site was not glycosylated. All disulfide bonds were within individual peptides showing that the domain was stabilized by intramolecular disulfide bonds and that CysD dimers were of non-covalent nature. These observations suggest that CysD domains act as non-covalent cross-links in the MUC2 gel, thereby determining the pore sizes of the mucus.

Page Manager: Webmaster|Last update: 9/11/2012

The University of Gothenburg uses cookies to provide you with the best possible user experience. By continuing on this website, you approve of our use of cookies.  What are cookies?