he antigen (light green) is a peptide from a tumor cell, bacteria or virus. Dendritic cells present antigens to lymphocytes through their membran bound MHC-molecules (orange). After binding to the MHC-antigen complex, the T-cell receptor (violet) sends a signal cascade into the T-lymphocyte cell, that activates an immune response.

MHC or Major Histocompatibility Complex is a group of genes, present on the cell surface and carries a major role in immune response. This gene is present in chromosome 6. This MHC is three types- MHC I, MHC II, MHC III.

Structure of MHC I (Major Histocompatibility complex I)

MHC I is activated by intracellular protein (viral protein). MHC I, is present in all nucleated cells except sperm cell, play a crucial role in immune response.

This complex consists of the alpha (α) chain, which is heavy (chromosome 6) and beta (β) chain, which is light (chromosome 15). Alpha chain is made up of three subunits- α1, α2 (carbohydrate domain), α3 and beta is only one microglobulin β2. There is a non covalent interaction between α3 and β2. .

The structure of MHC I is as follows:-

The structure of MHC (Major Histocompatibility complex) I, shows every subunits
Structure of MHC (Major Histocompatibility Complex) I

The comparative study of α and β chains of MHC I :

Featuresα chain β chain
1) Variable α1, α2none
2) Constantα3 <– CD8 (binds to TH cell)β2
3) Nature IntegralPeripheral
4) Most conservedα3none
5) Molecular weight (KD)4512
6) Number of Amino acids340-350100
7) CD 8 binding site α3none
8) Chromosome number 615
9) Glycosylation α2none
10) Protein binding site α1, α2none
11) Type of chainHeavyLight
Features of α and β chain

Peptides that binds to MHC I:

The peptide should be 8-10 amino acids long. The concept will be more understandable by the picture below:

The image shows in which position a protein can bind of Major Histocompatibility complex I.
A peptide binds to MHC I

Treatment of MHC I by the followings:

  1. In SDS- PAGE, two bands are obtained. One is a thick band, consists of all the α subunits. Another one is thin of β2.
  2. After digestion by papain, two parts, which is shown in the picture below. Papain always cut 13 amino acids above from the cell membrane.
  3. After digestion by pepsin, multiple fragments are obtained.
MHC I in SDS-PAGE, Papain and pepsin

Structure of MHC II (Major Histocompatibility complex II)

MHC II is activated by extracellular protein (bacterial protein). MHC II, is mainly present on APC (Antigen presenting cells). It always lacks in nerve cell, play a crucial role in immune response.

This complex consists of the alpha (α) chain (chromosome 6) and beta (β) chain (chromosome 6). Alpha chain is made up of two subunits- α1, α2 and beta is made up of two subunits- β1, β2. There are two non covalent interactions between α and β.

The structure of MHC II is as follows:-

The structure of MHC II

The comparative study of α and β chains of MHC I :

Featuresα chainβ chain
1) Domainα1, α2β1, β2
2) Glycosylationboth β1
3) Variable domainα1β1
4) Constant domainα2β2
5) Chromosome 66
6) Polymorphismα1β1
7) CD4noneβ2
8) Peptide bindingα1β1
The features of α and β chains of MHC II

Peptides that binds to MHC I:

The peptide should be 24 amino acids long. The concept will be more understandable by the picture below:

Pattern of peptide binding in MHC II

Treatment of MHC II by the followings:

  1. In SDS- PAGE, two bands are obtained. Both are similar bands.
  2. After digestion by papain, three parts, which is shown in the picture below. Papain always cut 13 amino acids above from the cell membrane.
  3. After digestion by pepsin, multiple fragments are obtained.
MHC II digestion

[HLA-DR determinants code for class II MHC. ]

Structure of MHC III (Major Histocompatibility Complex III)

The features are as follows:

  1. It is a secretory protein.
  2. It has no role in antigen presentation.
  3. It has no structural similarities with MHC I and MHC II.
  4. It plays a crucial role in immune response.
  5. it provides cytokines (TNFα), complement factor (C2, C4 and factor B), hydrolytic enzymes and HSP (Heat shock proteins).

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