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・ Complement factor I
・ Complement fixation test
・ Complement graph
・ Complement membrane attack complex
・ Complement of HMS Bounty
・ Complement receptor
・ Complement receptor 1
・ Complement receptor 2
・ Complement receptor of the immunoglobulin family
・ Complement set email filtering
・ Complement system
・ Complementarianism
・ Complementarity
・ Complementarity (molecular biology)
・ Complementarity (physics)
Complementarity determining region
・ Complementarity theory
・ Complementary and Alternative Medicine Program
・ Complementary and Integrated Medicine Research Unit, University of Southampton
・ Complementary and Natural Healthcare Council
・ Complementary assets
・ Complementary cells
・ Complementary code keying
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Complementarity determining region : ウィキペディア英語版
Complementarity determining region

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. As the most variable parts of the molecules, CDRs are crucial to the diversity of antigen specificities generated by lymphocytes.
==Location and structure==

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. 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''. 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. 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. and more recently by North et al. 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.

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