Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG)
The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).
Feature 1:Fab binding site [polypeptide binding site]
Evidence:
Structure:1PKQ_E; Rat MOG extracellular domain interacts with antigen binding fragment (Fab) of mouse monoclonal antibody,8-18C5; contacts based on 3.5 A distance.
Comment:In rat MOG, a strained ligand-binding loop forms the upper edge of the binding site. It has been reported that the sequence of this loop, RDHSYQEE, appears unique for MOG.
Jiyao W et al.(2023). "The conserved domain database in 2023.",