cd20989

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains

CDD entry
Member databaseCDD
CDD typedomain
Short nameIgV_1_Nectin-2_NecL-5_like_CD112_CD155
SetIg

Description

The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.
[5, 9, 8, 1, 6, 7, 2, 3, 4]

References

1.Cell adhesion molecules 1: immunoglobulin superfamily. Brummendorf T, Rathjen FG. 2, 963-1108, (1995). PMID: 8574878

2.Preliminary crystallographic characterization of the human beta2 microglobulin His31Tyr mutant in a tetrameric assembly. Zuccotti S, Rosano C, Mangione P, Bellotti V, Bolognesi M. Acta Crystallogr. D Biol. Crystallogr. 59, 1270-2, (2003). View articlePMID: 12832782

3.Structural determinants in the sequences of immunoglobulin variable domain. Chothia C, Gelfand I, Kister A. J. Mol. Biol. 278, 457-79, (1998). View articlePMID: 9571064

4.Canonical structures for the hypervariable regions of immunoglobulins. Chothia C, Lesk AM. J. Mol. Biol. 196, 901-17, (1987). View articlePMID: 3681981

5.The immunoglobulin fold. Structural classification, sequence patterns and common core. Bork P, Holm L, Sander C. J. Mol. Biol. 242, 309-20, (1994). PMID: 7932691

6.The immunoglobulin superfamily--domains for cell surface recognition. Williams AF, Barclay AN. Annu. Rev. Immunol. 6, 381-405, (1988). PMID: 3289571

7.The immunoglobulin fold family: sequence analysis and 3D structure comparisons. Halaby DM, Poupon A, Mornon J. Protein Eng. 12, 563-71, (1999). View articlePMID: 10436082

8.Evolution of antigen binding receptors. Litman GW, Anderson MK, Rast JP. Annu. Rev. Immunol. 17, 109-47, (1999). View articlePMID: 10358755

9.The immunoglobulin superfamily: an insight on its tissular, species, and functional diversity. Halaby DM, Mornon JP. J. Mol. Evol. 46, 389-400, (1998). View articlePMID: 9541533

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