CMB1003/L23 Humoral Specific Immunity II Flashcards
What are the 2 types of light chains on antibodies?
Kappa or lambda
What are the domains of the heavy chain on antibodies? (2)
C(H)1-3
V(H)
What are the domains of the light chain on antibodies? (2)
C(L)
V(L)
What is the domain of the glycosylated H chains on antibodies?
C(H)2
Define the term ‘domain’.
Compactly folded globular units within proteins, often with evolutionary significance
The domains found in Ig are also found in which other molecules involved in immunity? (3)
T cell receptor
MHC molecules
Various cell adhesion molecules
Signalling molecules
Describe the structure of C(L) and V(L) domains. (4)
Compact immunoglobulin domains
100-110 amino acids
2 sheets of B strands
Intra-chain disulphide bond
What are hypervariable (HV)/ complementary-determining regions (CDR)? (3)
3 loops of HV on each H and L chain
6 CDR form the antigen binding sites
Framework (other loops and strands) less variable
What do the C domains control?
Effector function of Ig
What are the 5 heavy chain isotypes of antibodies?
Mu/ IgM
Delta/ IgD
Gamma/ IgG
Epsilon/ IgE
Alpha/ IgA
What is the functional difference between kappa and lambda light chains?
None
What are the macro structures of the 5 isotypes?
IgG, IgD, IgE simple
IgA forms a dimer
IgM forms a pentamer
Describe the structure of IgM. (3)
Mew chains
5 domains
No hinge
(Mew2L2)5 covalently bound to J chain
What is the valency of IgM?
10
Describe the affinity of IgM. (2)
First response
Relatively low affinity as pre-affinity maturation