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  Domain Name: IgV
Immunoglobulin variable domain (IgV). IgV: Immunoglobulin variable domain (IgV). Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 27
Total Disease Mutations Found: 5
This domain occurred 34 times on human genes (72 proteins).



  AGAMMAGLOBULINEMIA 6
  AND CATARACTS
  BLOOD GROUP--LUTHERAN NULL
  CD8 DEFICIENCY, FAMILIAL
  HEMORRHAGIC DESTRUCTION OF THE BRAIN, SUBEPENDYMAL CALCIFICATION,


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 The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs.

 Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below.



Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
heterodimer interface
antigen binding site
L1 hypervariable region
L2 hypervariable region
L3 hypervariable region











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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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