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Printable Handouts
Navigable Slide Index
- Introduction
- Introduction to antibody structure
- Schematic of IgG structure
- Antibody fragments
- Schematic view of IgG domains
- Flexibility of the IgG molecule
- Immunoglobulin C-region domain structure
- Immunoglobulin V-region domain structure
- Ribbon backbone model of IgG
- Space filling model of IgG
- Mammalian antibody classes
- Immunoglobulin subclasses
- Antibody isotypes in human, mouse and rat
- IgM monomer and pentamer
- IgA monomers and dimers
- Immunoglobulin IgD and IgE
- Cell surface immunoglobulin
- Thank you for listening
Topics Covered
- The basic antibody structure
- Mammalian antibody classes
- Immunoglobulin subclasses
- Structure of different subclasses and classes of antibody
- Soluble and cell-surface antibodies
Links
Series:
Categories:
Therapeutic Areas:
Talk Citation
Clark, M. (2021, February 28). Antibody structure and function: antibody structure [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 3, 2024, from https://doi.org/10.69645/WQIO6778.Export Citation (RIS)
Publication History
Financial Disclosures
- Requested.
Antibody structure and function: antibody structure
Published on February 28, 2021
34 min
Other Talks in the Series: The Immune System - Key Concepts and Questions
Transcript
Please wait while the transcript is being prepared...
0:00
Hi, my name is Dr. Mike Clark,
and I was formerly Reader in Therapeutic Molecular Immunology
at the Department of Pathology, Cambridge University.
This lecture is going to be about antibody structure and
function and is going to be divided into two parts.
In part 1 of the lecture,
I'm going to deal with the structures.
0:17
Immunology presents us with a real problem,
and that is that we don't know in advance
what infectious diseases we will encounter during our lifetime.
We're going to be faced with a vast array of
different pathogens that will infect us at different times during our life.
Each of those different pathogens will present us with
an array of different antigens that they express,
and we will have to make an immune response that deals with all those different antigens.
This is the problem of the generation of diversity in the formation of antibodies.
We need to have antibodies that are specific to
all the different antigens that we might encounter during our lifetime.
In this lecture, we're going to,
first of all, deal with the basic antibody structure.
This is the structure of the standard antibody,
its variable regions that bind to these different antigens,
and then the constant regions.
Then we'll go on to deal with the structure of different classes and subclasses of
antibody that will mediate
the different functions that we will deal with in the next lecture.
1:12
What we have here is the schematic of an IgG structure,
and I think many of you will be familiar with this.
It's a basic Y-shaped molecule that is depicted in many publications.
This is really the basic structure of the IgG molecule as I show here,
the one that's most commonly discussed.
What you can see is that the molecule has effectively a certain symmetry about it.
It's actually a pseudo-axis of
rotational symmetry about the vertical axis in this picture.
What you can see is we've got an antigen-binding site indicated on the top right here,
and there are actually two antigen-binding sites
in this molecule: one on the left and one on the right.
We've got various domains,
these are protein domains that make up the entire structure.
Each of these is delineated by those ellipses on the screen.
The molecule is made up of two heavy chains and two light chains.
These have got domains which are given letters and numbers.
We can see here that we've got domains on the heavy chain,
'H' for heavy chain,
which are labeled in this diagram: VH,
CH1, CH2, and CH3.
These stand for the variable domain of the heavy chain:
the first constant domain of the heavy chain,
the second constant domain of the heavy chain,
and the third constant domain of the heavy chain.
Then we've got two other domains up here which are from the light chain.
We've got the variable domain of
the light chain and the constant domain of the light chain.
These are like beads on a string in terms of the protein structure,
and the molecule is built up from repeated domains within the structure.
Between the heavy chain 1 and the heavy chain 2 domains,
there is actually, in this particular molecule, the IgG,
there is a more flexible region which is called the hinge.
This is, rather the domain,
is a more flexible long protein chain that joins the two domains together.
Then finally, an indicator on this diagram we've got a glycosylation site,
which is commonly conserved in the CH2 region of the IgG molecule.
So that's the basic structure and you'll come across
this representation over and over again when you look at it,
and we'll be referring back to these types of diagrams as we go on with the discussion.
It's worth thinking about this in terms of, as I pointed out,
you've got a certain repeated structure within it and
repeating domains building up the entire subject.
Also, you've got the rotational symmetry within this molecule,
that the two halves of the molecule;
if you rotate the right-hand side and rotate it over to the left, essentially,
you've got identical heavy and light chains on
each side of this molecule but rotated through a 180 degrees.