Antibody Structure 2 & Response Flashcards
What are the two types of light chains? What are the functional regions of these chains?
Kappa or lambda
Functional regions: 2 domains. 1) Variable 2) Constant
What are the two types of disulfide bonds in an Ig? Which is more constant?
Interchain and intrachain. Intrachain is almost always the same.
What are the classes of heavy chain for each Ig class?
A - alpha D - delta G - gamma E - epsilon M - mu
What are the four domains of an IgG heavy chain?
One variable domain and the N terminus, then 3 constant domains
One constant + variable = Fab
2 constant = Fc
What is the purpose of the hinge region?
Between constant domains 1 and 2 of heavy chain, allows for flexibility of Ig binding.
Where do carbohydrates attach to Ig’s?
To the second constant domain of the heavy chain, which is the first part of Fc
What is Fv?
The smallest fragment which retains site for Ag reaction. The two variable domains of heavy and light chain
What does Papain vs Pepsin fragmentation do? Why is this significant?
Papain - Breaks at hinge, leaving 2 Fab and 1 Fc
Pepsin - breaks in the Fc region, losing Fc function (how Fc function was determined)
What are the Fc functions?
Complement fixation
Cell binding
Transplacental passage (IgG functionality)
What is the only multimeric Ig?
IgA, as it normally exists in two forms in the serum
Monomeric (7S, like IgG)
Polymeric - normal and secretory form
Heavy chain has alpha1 and alpha 2 subclasses
What is the purpose of the J chain for IgM and IgA?
Joining chain - holds together than individual Ig monomers to make the larger structure (pentamer and dimer respectively)
Which Ig was the first to evolve, and what are its functions? How many domains does its heavy chain have?
IgM, involved in agglutination and serum primary response.
Has a 5th domain (4th constant region) for attachment to J chain to make pentamer
What is IgD structure and where does it exist?
It is a monomer which has a partial 5th domain (slightly larger than IgG) - mostly exists on cell surfaces, especially developing or anergic B cells
What is the structure of IgE and how many domains does it have?
monomer, stays attached to mast cell surfaces most of the time but can be free. Involved in immediate hypersensitivity
Has one extra domain (4th constant) for attachment to cell
Do the dimensions of the antigen binding site vary for different antibodies?
Yes
Where do contact residues exist? About what percent do they make up?
In the Variable regions of the heavy and light chains
Make up about 6% of the Ig
What are CDRs / Hvs and how were they determined? What is between them?
CDR = complementarity determining region
Hv = hypervariable region
same thing
Determined via sequence analyses of antibodies made from myeloma patients producing all the same B cells and hence Ig class
In between them: framework regions