Immunoglobulin family

A beta barrel is a three-dimensional protein fold motif in which beta strands connected by loops form a barrellike structure. For example, this fold motif is found in many proteins of the immunoglobulin family and of the chymotrypsin family of serine proteases. 

RAGE, (domains V, Cl, and C2) belongs to the immunoglobulin family of proteins. 

Soluble antigen receptors, which are formed by activated B cells (plasma cells see p. 294) and released into the blood, are known as antibodies. They are also members of the immunoglobulin family (Ig see p. 296). Antibodies are an important part of the humoral immune defense system. They have no antimicrobial properties themselves, but support the cellular immune system in various ways ... 

Other cell adhesion molecules. Long before the discovery of integrins another class of transmembrane adhesion molecules were recognized as members of the immunoglobulin family. These were called cell... 

Crossin KL, Krushel LA. Cellular signaling by neural cell adhesion molecules of the immunoglobulin family. Dev Dyn 2000 21 8260-8279. 

Molecular chaperone (relative molecular mass 78 K) found in the lumen of the ER. BiP is related to the Hsp70 family of heat-shock proteins and was originally described as immunoglobulin heavy chain binding protein. 

Immunoglobulins A, E, G, M IgG I Immunc obulin G class 1 IgGa, Immunoglobulin G class 2a IGF-I Insulin-like growth factor Ig-SF Immunoglobulin supergene family... 

FIGURE 7-1 The immunoglobulin (Ig) gene family of molecules. Several varieties of Ig domain-containing molecules are contained within the Ig gene superfamily. Most are type I membrane proteins some have only Ig domains or other moieties that may convey function (see text). V, variable Ig domain C, constant Ig domain MAG, myelin-associated glycoprotein NCAM, neural cell adhesion molecule GPI, glycosylphosphatidyl-inositol EC, extracellular domain FN, fibronectin. 

Kelm, S., Pelz, A., Schauer, R. etal. Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily. Curr. Biol. 4 965-972,1994. 

Abe, J., Suzuki, H Notoya, M Yamamoto, T., and Hirose, S. (1999) Ig-hepta, a novel member of the G protein-coupled hepta-helical receptor (GPCR) family that has immunoglobulin-like repeats in a long N-terminal extracellular domain and defines a new subfamily of GPCRs. J. Biol. Chem. 274,19957-19964. 

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