2 IG structure Flashcards
what is b cell receptor
antibody
will not go from membrane bound to soluble BCR unless
you get infection
specificity of epitope on BCR will not change when it is
soluble
every antibody has how many antigen binding site
2
what are two functional roles of b cell receptor
looks for antigen
secretes antibody
immunoglobulin is
antibody
Ab or Ig means
antibody
neutralizing antibodies
bind microbe or toxin and block them from entry
enhance innate cell function how
complement with antibody works better
what is big difference b/w BCR on surface of receptor and the secreted form
there is transmembrane region that will not be present in secreted form of antibody
BCR with transmembrane region will
stay on surface of b cell ,will be BCR
what is basic structure of antibody
heavy chain and light chain
antibody contains how many heavy and light chains
two identical light chains
two identical heavy chains
variable region on antibody is involved in
binding to antigen
constant region of antibody is involved in
mediating effector functions
antigen binding site of antibody is combinatino of
variable region of heavy and light chain - so they will both contribute to antigen binding site
resting b cell what will happen to most of them
they live until they die and they never find their “partner”
mature naive b cell must express what on surface
must express both IgM and IgD on surface
domain within light chain
constant and variable domain
domain within heavy chain
3 or 4 constant domains and 1 variable domain
Fab
portion that is antigen binding on antibody
Fc
portion that is constant on antibody
heavy chain has how many constant regions
3
light chain has how many constant regions
1
each domain in antibody is
immunoglobulin domain
connecting Fc to Fab fragment
hinge region
hinge region
antibody is flexible, hinge connects Fc to Fab fragments
what does hinge flexibilty allow
antibody to bind antigen close together, far apart, moving
antibodies recognize almost how many antigenic determinants
infinite number
what portion recognizes the antigen
variable region
hypervariable region
determines specificity within variable domain
CDR stands for
complementarity determining region
what is magic number for CDR
3
there are how many hypervariable regions
3
how many hypervariable chains in heavy and light chain
3 in each
what region has the variablity in antibody
v region
what type of interaction does epitope have with zika virus
electrostatic forces hydrogen bonds van der waals forces hydrophobic forces NOT covalent
epitope does not have what kind of bond with antigen
no covalent bond
dissociation constant of 10^-12 is what affinity
very strong
dissociation constant of 10^-4 is what affinity
relatively weak but still have interaction
even though no covalent bond b/w antigen and antibody, it is still
a very strong bond b/c of all the forces
avidity
one single interaction of one antigen binding site with one epitope on
one that binds two is stronger than one that binds two.
avidity is combination of all the different interactions
once an antibody binds a particular pathogen what does it do
complement system more efficiently activated. C1 can bind directly to antibody molecule - the Fc region
IgM is a
pentimer
IgM has how many binding site
10
if a b cell is ready for action (to mature) it will have how many different antibodies on surface
2
IgM and IgD
isotype switching only happens
after infection
describe clonal selection with IgM and IgG
our body already has antibodies for things that will help get rid of diseases we’ve never seen
What are the major classes of immunoglobulin
IgG M D A E
Fc is made up of
heavy chain