Monday, December 23, 2013

Igg1 Structure And Function

Immunoglobulin G1 Functional Properties Basic Structural Properties In this hand out I will be focusing on the companionable system of the most abundant type of immunoglobulin, Immunoglobulin G1 (IgG1), and how these colonial body parts explain its utilitarian properties. The IgG1 is a tetrameric quartet structure, with ii indistinguishable light handcuffs and cardinal identical heavy ambits, which a8re linked to take onher by disulphide bonds (Figure 1a). Each IgG1 contains two Fab moieties, consisting of two inconsistent and two constant domains per Fab. The variable Fab domains shape the paratope at the amino group perch of the monomer. Constant domains have a characteristic structure cognize as the immunoglobulin fold, a well hold motive in all Beta class domains [1]. The back up and third constant domains of the two heavy drawstrings, in the quest after voice of the IgG1, make up the Fc field of the antibody. This sphere binds to confused Fc recepto rs on effector cells to activate various glade mechanisms, much(prenominal) as antigen dependent cellular cytotoxicity (ADCC) [2]. Attached to the Fc region of one by one heavy filament is a complex oligosaccharide, which is bonded to the heavy fibril 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).
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The oligosaccharide has been appearingn 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 h as been show in studies by testing the affin! ity of human Fc receptors with disparate 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 consummate 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 pull in a full essay, order it on our website: BestEssayCheap.com

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