World Library  
Flag as Inappropriate
Email this Article

Conformational Epitope

Article Id: WHEBN0018159480
Reproduction Date:

Title: Conformational Epitope  
Author: World Heritage Encyclopedia
Language: English
Subject: Antigen, Clonal deletion, Allotype (immunology), Isotype (immunology), Immune complex
Publisher: World Heritage Encyclopedia

Conformational Epitope

Recognition of conformational epitopes by B cells. Note how the segments widely separated in the primary structure have come in contact in the three-dimensional tertiary structure forming part of the same epitope[1]

A conformational epitope is a sequence of sub-units (usually, amino acids) composing an antigen that come in direct contact with a receptor of the immune system.

An antigen is any substance that the immune system can recognize as foreign. Antigens are usually proteins that are too large to bind as a whole to any receptor so only specific segments, that form the antigen, bind with a specific receptor. Such segments are called epitopes. Likewise, it is only paratope of the receptor that comes in contact with the epitope.

Proteins are composed of repeating nitrogen-containing subunits called amino acids that in nature do not exist as straight chains called primary structure, but as folded whorls with complex loops. The latter is known as the tertiary structure of a protein. So, whenever a receptor interacts with an undigested antigen, the surface amino acids that come in contact may not be continuous with each other if the protein is unwound. Such discontinuous amino acids that come together in three-dimensional conformation and interact with the receptor's paratope are called conformational epitopes. In contrast, if the antigen is digested, small segments called peptides are formed, which bind with major histocompatibility complex molecules, and then later with T cell receptors through amino acids that are continuous in a line. These are known as linear epitopes.[1]

See also

  • EpiSearch, A new method to Predict conformational epitopes using phage display peptide sequences. The method is available online at


  1. ^ a b

External links

  • Antibody-protein interactions: benchmark datasets and prediction tools evaluation

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.