Complementarity-determining region
Fab region) of an antibody. The complementarity-determining regions of the heavy chain are shown in red (PDB: 1IGT
).Complementarity-determining regions (CDRs) are part of the variable chains in
lymphocytes
.
Location and structure
variable domains
shown in blue, and the CDRs (which are part of the variable domains) in light blue.There are three CDRs (CDR1, CDR2 and CDR3), arranged non-consecutively, on the
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 regions.[1] Within the variable domain, CDR1 and CDR2 are found in the variable (V) region of a polypeptide chain, and CDR3 includes some of V, all of diversity (D, heavy chains only) and joining (J) regions.[2] CDR3 is the most variable.
The
tertiary structure of an antibody is important to analyze and design new antibodies. The three-dimensional structures of the non-H3 CDRs of antibodies have been clustered and classified by Chothia et al.[3] and more recently by North et al.[4] Homology modeling is a computational method to build tertiary structures from amino-acid sequences. The so-called H3-rules are empirical rules to build models of CDR3.[5]
See also
References
- ISBN 0-7216-0008-5.
- ISBN 978-0-7817-6519-0.
- PMID 9367782.
- PMID 21035459.
- PMID 10428499.
External links
- Complementarity+determining+regions at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- PyIgClassify -- server for classification of CDR conformations