D
IPR007110

Immunoglobulin-like domain

InterPro entry
Short nameIg-like_dom
Overlapping
homologous
superfamilies
 
domain relationships

Description

The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulphide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha, delta, epsilon, gamma and mu, all consisting of a variable domain (VH) and three (in alpha, delta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins, in which the variable and constant domains have clear, conserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable;
IPR013106
), C1-set (constant-1;
IPR003597
), C2-set (constant-2;
IPR008424
) and I-set (intermediate;
IPR013098
)
[1]
. Structural studies have shown that these domains share a common core Greek-key β-sandwich structure, with the types differing in the number of strands in the β-sheets as well as in their sequence patterns
[4, 3]
.

Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions, including cell-cell recognition, cell-surface receptors, muscle structure and the immune system
[2]
.

References

1.Sequence profiles of immunoglobulin and immunoglobulin-like domains. Smith DK, Xue H. J. Mol. Biol. 274, 530-45, (1997). View articlePMID: 9417933

2.Immunoglobulin superfamily proteins in Caenorhabditis elegans. Teichmann SA, Chothia C. J. Mol. Biol. 296, 1367-83, (2000). View articlePMID: 10698639

3.Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state. Fowler SB, Clarke J. Structure 9, 355-66, (2001). View articlePMID: 11377196

4.Protein--protein recognition: juxtaposition of domain and interface cores in immunoglobulins and other sandwich-like proteins. Potapov V, Sobolev V, Edelman M, Kister A, Gelfand I. J. Mol. Biol. 342, 665-79, (2004). View articlePMID: 15327963

Cross References

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