Complementarity-determining regions (CDRs) are part of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively, where these molecules bind to their specific antigen. A set of CDRs constitutes a paratope. As the most variable parts of the molecules, CDRs are crucial to the diversity of antigen specificities generated by lymphocytes.
The "upper" part (Fab region) of an antibody. The complementarity-determining regions of the heavy chain are shown in red (PDB: 1IGT).
Sketch of an antibody with the 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 amino acid sequence of a variable domain of an antigen receptor. Since the antigen receptors are typically composed of two variable domains (on two different polypeptide chains, heavy and light chain), there are six CDRs for each antigen receptor that can collectively come into contact with the antigen. A single antibody molecule has two antigen receptors and therefore contains twelve CDRs total. There are three CDR loops per variable domain in antibodies. Sixty CDRs can be found 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 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]
^Abbas AK and Lichtman AH (2003). Cellular and Molecular Immunology (5th ed.). Saunders, Philadelphia. ISBN0-7216-0008-5.
^William E. Paul (2008). Fundamental Immunology (6th ed.). Lippincott Williams & Wilkins. ISBN978-0-7817-6519-0.
^Al-Lazikani, B.; Lesk, A. M.; Chothia, C. (1997). "Standard conformations for the canonical structures of immunoglobulins". Journal of Molecular Biology. 273 (4): 927–948. doi:10.1006/jmbi.1997.1354. PMID 9367782.
^North, B.; Lehmann, A.; Dunbrack Jr, R. L. (2011). "A New Clustering of Antibody CDR Loop Conformations". Journal of Molecular Biology. 406 (2): 228–256. doi:10.1016/j.jmb.2010.10.030. PMC3065967. PMID 21035459.
^Shirai, H; Kidera, A; Nakamura, H (1999). "H3-rules: identification of CDR-H3 structures in antibodies". FEBS Letters. 455 (1–2): 188–97. doi:10.1016/S0014-5793(99)00821-2. PMID 10428499.
External linksedit
Complementarity+determining+regions at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
PyIgClassify -- server for classification of CDR conformations
November 11, 2023
complementarity, determining, region, cdrs, part, variable, chains, immunoglobulins, antibodies, cell, receptors, generated, cells, cells, respectively, where, these, molecules, bind, their, specific, antigen, cdrs, constitutes, paratope, most, variable, parts. Complementarity determining regions CDRs are part of the variable chains in immunoglobulins antibodies and T cell receptors generated by B cells and T cells respectively where these molecules bind to their specific antigen A set of CDRs constitutes a paratope As the most variable parts of the molecules CDRs are crucial to the diversity of antigen specificities generated by lymphocytes The upper part Fab region of an antibody The complementarity determining regions of the heavy chain are shown in red PDB 1IGT Contents 1 Location and structure 2 See also 3 References 4 External linksLocation and structure edit nbsp Sketch of an antibody with the 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 amino acid sequence of a variable domain of an antigen receptor Since the antigen receptors are typically composed of two variable domains on two different polypeptide chains heavy and light chain there are six CDRs for each antigen receptor that can collectively come into contact with the antigen A single antibody molecule has two antigen receptors and therefore contains twelve CDRs total There are three CDR loops per variable domain in antibodies Sixty CDRs can be found 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 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 editFramework region Hypervariable regionReferences edit Abbas AK and Lichtman AH 2003 Cellular and Molecular Immunology 5th ed Saunders Philadelphia ISBN 0 7216 0008 5 William E Paul 2008 Fundamental Immunology 6th ed Lippincott Williams amp Wilkins ISBN 978 0 7817 6519 0 Al Lazikani B Lesk A M Chothia C 1997 Standard conformations for the canonical structures of immunoglobulins Journal of Molecular Biology 273 4 927 948 doi 10 1006 jmbi 1997 1354 PMID 9367782 North B Lehmann A Dunbrack Jr R L 2011 A New Clustering of Antibody CDR Loop Conformations Journal of Molecular Biology 406 2 228 256 doi 10 1016 j jmb 2010 10 030 PMC 3065967 PMID 21035459 Shirai H Kidera A Nakamura H 1999 H3 rules identification of CDR H3 structures in antibodies FEBS Letters 455 1 2 188 97 doi 10 1016 S0014 5793 99 00821 2 PMID 10428499 External links editComplementarity determining regions at the U S National Library of Medicine Medical Subject Headings MeSH PyIgClassify server for classification of CDR conformations Retrieved from https en wikipedia org w index php title Complementarity determining region amp oldid 1140729007, wikipedia, wiki, book, books, library,
