Difference between revisions of "Part:BBa K3064009"
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Latest revision as of 18:32, 23 October 2020
mmuIgG-Fc
Immunoglobulin G (IgG) is a type of antibody, containing the fragment crystallizable region(Fc).
Usage and Biology
As a type of antibody, IgG binds many kinds of pathogens and protects the body from infection. IgG shapes like a Y due to its tetrameric quaternary structure, with two identical class heavy chains and two identical light chains. On the bottom of the heavy chain is the Fc domain. Fc mediates different physiological effects of antibodies by interacting with various cell receptors and complement proteins.1 Also, it can be recognized and bound with TRIM21,an E3 ubiquitin-protein ligase that has been applied to a protein degradation method known as Trim-Away.
In our project, this part is linked with glucagon. Glucagon binds to glucagon receptor(GCGR), Fc domain recruits the TRIM21, leading to the ubiquitination and final degradation of GCGR.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 7
References
1.Paul, William. Fundamental Immunology (Seventh ed.). Lippincott Williams & Wilkins. p. 1401–142. ISBN 978-1451117837.(2015)
MIT_MAHE 2020
Summary
As a type of antibody, IgG binds many kinds of pathogens and protects the body from infection. IgG shapes like a Y due to its tetrameric quaternary structure, with two identical class heavy chains and two identical light chains. On the bottom of the heavy chain is the Fc domain. Fc mediates different physiological effects of antibodies by interacting with various cell receptors and complement proteins.
References
1. Paul, William. Fundamental Immunology (Seventh ed.). Lippincott Williams & Wilkins. p. 1401–142. ISBN 978-1451117837.(2015)