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Publication : Channel catfish soluble FcmuR binds conserved linear epitopes present on Cmu3 and Cmu4.

First Author  Nayak DK Year  2010
Journal  Mol Immunol Volume  47
Issue  6 Pages  1306-16
PubMed ID  20031218 Mgi Jnum  J:221557
Mgi Id  MGI:5640948 Doi  10.1016/j.molimm.2009.11.026
Citation  Nayak DK, et al. (2010) Channel catfish soluble FcmuR binds conserved linear epitopes present on Cmu3 and Cmu4. Mol Immunol 47(6):1306-16
abstractText  A linear epitope on catfish IgM has been identified as the docking site for the catfish soluble FcmuR (IpFcRI). Western blot analyses and latex bead binding assays identified the consensus octapeptide motif FxCxVxHE located at the second cysteine that forms the intrachain disulfide bond of the catfish Cmu3 and Cmu4 immunolglobulin (Ig) domains as the IpFcRI binding sites. Furthermore, molecular modeling of catfish Cmu3 and Cmu4 confirmed that the octapeptide in both of these domains is accessible for IpFcRI interactions. In addition, since this octapeptide motif is also found in other vertebrate Ig domains, IpFcRI binding to Ig heavy (H) and light (L) chains from rainbow trout, chicken, mouse, rabbit, and goat were examined by Western blot analyses and latex bead binding assays. IpFcRI readily bound reduced rainbow trout (Igmu), chicken (Ignu), mouse (Igmu, Iggamma1, Iggamma2a, Iggamma2b, and Igalpha), rabbit (Igmu and Iggamma) and goat (Iggamma) IgH chains, and mouse Igkappa and Iglambda, and chicken Iglambda IgL chains. IpFcRI also bound mouse IgM, IgA and IgG subclasses when examined under native conditions.
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