Igg1 Structure And Function

Immunoglobulin G1
Functional Properties
Basic Structural Properties
In this circulate I will be focusing on the social system of the most abundant type of immunoglobulin, Immunoglobulin G1 (IgG1), and how these complex body parts explain its utilitarian properties. The IgG1 is a tetrameric quaternary structure, with ii identical light handcuffs and two identical heavy ambits, which a8re linked to take onher by disulphide bonds (Figure 1a). Each IgG1 contains two Fab moieties, consisting of two variable and two constant domains per Fab. The variable Fab domains shape the paratope at the amino group terminal of the monomer. Constant domains have a characteristic structure known as the immunoglobulin fold, a well hold motif in all Beta class domains [1]. The back up and third constant domains of the two heavy drawstrings, in the chase after voice of the IgG1, make up the Fc region of the antibody. This region binds to confused Fc receptors on effector cells to activate various clearing mechanisms, much(prenominal) as antigen dependent cellular cytotoxicity (ADCC) [2]. Attached to the Fc region of separately heavy chain is a complex oligosaccharide, which is bonded to the heavy chain at the Asn314 residue (Figure 1b).

Importance of Glycosylation
The IgG1 is glycosylated at the Asn314 of the heavy chain within the Fc region (Figure 1b).



The oligosaccharide has been shown to be vital for the affinity of the Fc region to the Fc receptors of the leukocytic cells of the immune system and other forms of biological recognition [3, 4]. This has been show in studies by testing the affinity of human Fc receptors with different glycoforms of IgG1-Fc and it was found that the glycoforms of IgG1-Fc which were partially de-glycosylated were several folds less active than the entire glycoforms [5].
There are numerous noncovalent interactions between the oligosaccharide and the protein moiety (Figure 2), and so resulting in reciprocal influences on each others conformation, playing an important role in protein...If you want to get a full essay, order it on our website: Orderessay



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