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. 2020 Apr 12;98(4):287–304. doi: 10.1111/imcb.12326

Table 3.

Unique features of IgG subclass Fc and hinge.

IgG subclass FcγR specificity Light‐chain attachment Hinge characteristics Fc stability Comment
IgG1 All FcγR Upper hinge Light‐chain attachment Stable Fc is >100× times more stable than IgG4 and IgG2.
Stable core hinge
IgG2 FcγRIIa His131 CH1 of Fab and/or upper hinge Stable core hinge with additional inter H‐chain disulfide bonds in the upper hinge. Unstable CH3:CH3 Alternative light‐chain attachment creates distinct conformers. Unlike IgG4, the CH3:CH3 instability does not lead to half‐molecule exchange as a result of stable core and upper hinge disulfides.
IgG4 FcγRI, FcγRIIb, FcγRIIc CH1 of Fab Labile core hinge Unstable CH3:CH3 Combined instability of core hinge and CH3:CH3 permits half‐IgG molecule exchange

Ig, immunoglobulin.