1h3v
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CRYSTAL STRUCTURE OF THE HUMAN IGG1 FC-FRAGMENT,GLYCOFORM (G2F)2,SG P212121
OverviewOverview
Antibodies may be viewed as adaptor molecules that provide a link between, humoral and cellular defence mechanisms. Thus, when antigen-specific IgG, antibodies form antigen/antibody immune complexes the effectively, aggregated IgG can activate a wide range of effector systems. Multiple, effector mechanisms result from cellular activation mediated through a, family of IgG-Fc receptors differentially expressed on leucocytes. It is, established that glycosylation of IgG-Fc is essential for recognition and, activation of these ligands. IgG antibodies predominate in human serum and, most therapeutic antibodies are of the IgG class.The IgG-Fc is a homodimer, of N-linked glycopeptide chains comprised of two immunoglobulin domains, (Cgamma2, Cgamma3) that dimerise via inter-heavy chain disulphide ... [(full description)]
About this StructureAbout this Structure
1H3V is a [Single protein] structure of sequence from [Homo sapiens]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity., Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P, J Mol Biol. 2003 Jan 31;325(5):979-89. PMID:12527303
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