Structure of Antibodies

Introduction

There are a lot of antibodies in our body. However, we seem not too much about it. We just simply remember that it is Y shape structure and it can fight the antigens. Therefore, we want to look more deeply about this topic to know how antibody can be produced and how it can produce a large number of antibodies. In this study, we will review the antibodies in different areas: Structure of antibody, ways of affecting the diversity of antibodies and mechanisms for generate antibodies and how to let it be specific. Moreover, we have a future direction for antibody technology development to talk a little bit for this area.

Structure of antibodies

As we all known that antibody is a type of protein with Y shape structure. It consists of two heavy chains and light chains (Roderick and Matthew, 2007). There are two types of light chains, which one is called Kappa and other is Lambda (Roderick, 2007). Both heavy and light chains connect with each other by using disulfide bonds. The function of hinge region can let antibodies become more fexible. Both heavy and light chain have variable region and constant region, variable region can give the specificity for binding antigen; while constant region (also name as isotype region) is determined the mechanism for destroy antigen, and guess the infection time by define the region of constant region of antibodies. As stated on USCSM(2010), hyper-variable region and framework region are similar meaning of the variable region and constant region.

Germ Line and Somatic Events

Heavy chain and light chain are come from a set of gene which can be express both variable and constant regions. Variable region contain three segments in heavy chain which are V, D and J. V stand for variable, D s...

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...ts become much different with each other so it can further increase the diversity of the antibodies.

Future Development and Conclusion

Due to special function of antibodies, we want to manufacture it to cure human against the antigens. However, in this moment to generate a specific antibodies is much waste time and the cost is very expensive. Therefore, in the future the products of antibodies will be common and popular.

To conclude, the antibodies synthesis is same as protein which is based on the central dogma: DNA makes mRNA then protein. The important points of changing functional activities for antibodies are at DNA section. In that sections there are a lot of methods to let antibodies become diversity and let antibodies much more specific. Moreover, the future development can make antibodies to treat the disease much more directly and not harmful to human.