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which are commonly used to differentiate the CDRs from each other. The structural relationship between different length CDRS is based on length-independent components, such as their sequence, and can further characterize CDRs. The loops, or three-dimensional structures of the non-H3 CDRs (all CDRs but H3) of antibodies have been clustered and classified by
Chothia et al. and more recently by North et al.
139:), 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
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of an antibody is important to analyze and design new antibodies. The structure and sequence of all six CDRs combined will determine the binding activity of the antigen receptor on an antibody or T-cell
Receptor. CDRs have been separated into canonical classes based on their varying loop lengths,
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Other factors contribute to the antibody-antigen interaction, including amino acid residues. Residues located in particular positions of a CDR loop are used to classify canonical structures. Uncharged-polar residues, especially Serine and
Tyrosine, are found in CDRs at a high concentration ratio.
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Antibody-antigen interactions are highly specific and those that have high affinity will interact with increased bond strength and trigger downstream immune responses. The strength of the bond between the epitope of the antigen and the paratope of the antibody will determine the affinity of the
165:. This rearrangement of the V-region is where the CDR-L3 and CDR-H3 are encoded and diversified, whereas the other four CDRs are generated in the germ-line. The diversification of the CDR-H3 will ultimately give antibodies their specificity, and ability to recognize antigens
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between the antigen and the antibody. Hydrogen bond interactions will induce the enzymatic activity of an enzyme; therefore, the more hydrogen bonds that are present at the antibody-antigen binding site will result in a stronger, more stable binding structure.
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of an antigen receptor. Three can be found on the Light-chain, named L1 through L3, and three on the Heavy-chain, named H1 through H3. Since the antigen receptors are typically composed of two variable domains (on two different polypeptide chains,
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of a polypeptide chain, and CDR3 includes some of V, all of diversity (D, heavy chains only) and joining (J) regions. CDR3 is the most variable. The V region sequence undergoes rearrangement during B-cell development, called
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respectively. CDRs are where these molecules bind to their specific antigen and their structure/sequence determines the binding activity of the respective antibody. A set of CDRs constitutes a
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Osajima T, Suzuki M, Neya S, Hoshino T (September 2014). "Computational and statistical study on the molecular interaction between antigen and antibody".
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molecule, which is composed of five antibodies and has increased avidity as a result of the collective affinity of all antigen-binding sites combined.
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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.
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Since most sequence variation associated with immunoglobulins and T cell receptors are found in the CDRs, these regions are sometimes referred to as
85:, or the antigen-binding site. As the most variable parts of the molecules, CDRs are crucial to the diversity of antigen specificities generated by
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260:"Antibody complementarity-determining regions (CDRs) can display differential antimicrobial, antiviral and antitumor activities"
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Al-Lazikani B, Lesk AM, Chothia C (November 1997). "Standard conformations for the canonical structures of immunoglobulins".
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Polonelli L, Pontón J, Elguezabal N, Moragues MD, Casoli C, Pilotti E, et al. (June 2008). El-Shemy HA (ed.).
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374:"Antibody complementarity-determining regions (CDRs): a bridge between adaptive and innate immunity"
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Gabrielli E, Pericolini E, Cenci E, Ortelli F, Magliani W, Ciociola T, et al. (December 2009).
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shown in blue, and the CDRs (which are part of the variable domains) in light blue.
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There are three CDRs (CDR1, CDR2 and CDR3), arranged non-consecutively, on the
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PyIgClassify -- server for classification of CDR conformations
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517:"H3-rules: identification of CDR-H3 structures in antibodies"
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These residues significantly contribute to the direct
468:"A new clustering of antibody CDR loop conformations"
65:) are polypeptide segments of the variable chains in
346:(6th ed.). Lippincott Williams & Wilkins.
466:North B, Lehmann A, Dunbrack RL (February 2011).
156:, CDR1 and CDR2 are found in the variable (V)
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515:Shirai H, Kidera A, Nakamura H (July 1999).
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321:(5th ed.). Saunders, Philadelphia.
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319:Cellular and Molecular Immunology
317:Abbas AK, Lichtman AH (2003).
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572:Medical Subject Headings
445:10.1006/jmbi.1997.1354
344:Fundamental Immunology
152:. Within the variable
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102:Location and structure
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163:somatic recombination
149:hypervariable regions
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201:Hypervariable region
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390:2009PLoSO...4.8187G
276:2008PLoSO...3.2371P
124:amino acid sequence
179:tertiary structure
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44:are shown in red (
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184:Homology modeling
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231:: 128–139.
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87:lymphocytes
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603:Immunology
598:Antibodies
587:Categories
207:References
38:Fab region
114:with the
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378:PLOS ONE
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190:See also
112:antibody
83:paratope
529:Bibcode
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272:Bibcode
79:T-cells
75:B-cells
574:(MeSH)
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177:The
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