Complementarity determining region

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A single chain antibody fragment showing the positions of the three complementarity determining regions, CDR1, CDR2 and CDR3
A single chain antibody fragment showing the positions of the three complementarity determining regions, CDR1, CDR2 and CDR3

A complementarity determining region (CDR) is a short amino acid sequence found in the variable domains of antigen receptor (e.g. immunoglobulin and T cell receptor) proteins that complements an antigen and therefore provides the receptor with its specificity for that particular antigen.

Each polypeptide chain of an antigen receptor contains three CDRs (CDR1, CDR2 and CDR3). Since the antigen receptors are typically composed of two polypeptide chains, there are six CDRs for each antigen receptor that can come into contact with the antigen (each heavy and light chain contains three CDRs), twelve CDRs on a single antibody molecule and sixty CDRs on a pentameric IgM molecule.

Since most sequence variation associated with immunoglobulins and T cell receptors are found in the CDRs, these regions are sometimes referred to as hypervariable domains.[1] Among these, CDR3 shows the greatest variability as it is encoded by a recombination of the VJ (VDJ in the case of heavy chain) regions.

[edit] References

  1. ^ Abbas AK and Lichtman AH (2003). Cellular and Molecular Immunology, 5th ed., Saunders, Philadelphia. ISBN 0-7216-0008-5. 

[edit] External links