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Kappa-chain immunoglobulin

Introduction

An antibody molecule. The two heavy chains are colored red and blue and the two light chains green and yellow. See also:[1]
Overview

Overview

A light chain is the small polypeptide subunit of an antibody (or immunoglobulin); a typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains.

In humans

In humans

There are two types of light chain in mammals,

  • lambda (λ) chain (1, 2, 3, and 4)
  • kappa (Îș) chain (only one type)
In other animals

In other animals

Other types of light chains can be found in lower vertebrates, such as the Ig-Light-Iota chain of Chondrichthyes and Teleostei.[1][2]

Camelids are unique among mammals as they have fully functional antibodies which have two heavy chains, but lack the light chains usually paired with each heavy chain.[3] The functional role of this separate repertoire is unknown as yet.

Structure

Structure

Only one type of light chain is present in a typical antibody, thus the two light chains of an individual antibody are identical.

Each light chain is composed of two tandem immunoglobulin domains:

  • one constant (IgC) domain
  • one variable domain (IgV) that is important for binding antigen

The approximate length of a light chain protein is from 211 to 217 amino acids.[1]

References

References

  1. ↑ 1.0 1.1 Janeway CA, Jr.; et al. (2001). Immunobiology (5th ed. ed.). Garland Publishing. (electronic full text via NCBI Bookshelf) ISBN 0-8153-3642-X.
  2. ↑ IMGT Index Antibodies (or Immunoglobulins).
  3. ↑ Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa E, Bendahman N, Hamers R (1993). “Naturally occurring antibodies devoid of light chains”. Nature. 363 (6428): 446–8. PMID 8502296.
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [2]