Light chain: Difference between revisions
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Latest revision as of 16:53, 9 August 2012
![[1]](http://www.emc.maricopa.edu/faculty/farabee/BIOBK/ANTIBODY.gif){kind=link}
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [2]
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
There are two types of light chain in mammals,
- lambda (λ) chain (1, 2, 3, and 4)
- kappa (κ) chain (only one type)
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
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
- ↑ 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.
- ↑ IMGT Index Antibodies (or Immunoglobulins).
- ↑ 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.
External links
- Immunoglobulin+Light+Chains at the US National Library of Medicine Medical Subject Headings (MeSH)