Biology, asked by Suraj111111, 1 year ago

Write an illustrated and detailed account on the structure of an IgG molecule

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Answered by swateesahu
11
Immunoglobulins are glycoprotein molecules that are produced by plasma cells in response to an immunogen and which function as antibodies.

GENERAL FUNCTION OF IMMUNOGLOBULINS:

Antigen binding :Immunoglobulins bind specifically to one or a few closely related antigens. antigen binding by antibodies is the primary function of antibodies and can result in protection of the host. 

Effector Functions Frequently the binding of an antibody to an antigen has no direct biological effect.

BASIC STRUCTURE OF IMMUNOGLOBULINS:

Heavy and Light Chains:All immunoglobulins have a four chain structure as their basic unit.

Disulfide bonds1. Inter-chain disulfide bonds
2. Intra-chain disulfide binds

Variable (V) and Constant (C) Regions
When the amino acid sequences of many different heavy chains and light chains were compared, it became clear that both the heavy and light chain could be divided into two regions based on variability in the amino acid sequences. THEY R
1. Light Chain 2. Heavy Chain 

D. Hinge Region
This is the region at which the arms of the antibody molecule forms a Y. It is called the hinge region because there is some flexibility in the molecule at this point.

E. Domains
Three dimensional images of the immunoglobulin molecule show that it is not straight as depicted . 
1. Light Chain Domains 2. Heavy Chain Domains 

F. Oligosaccharides
Carbohydrates are attached to the CH2 domain in most immunoglobulins. However, in some cases carbohydrates may also be attached at other locations.


All IgG's are monomers . The subclasses differ in the number of disulfide bonds and length of the hinge region.

hope this much helps

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