Posttranslational Modification and Human Disorders

G Brian Wisdom, The Queen's University, Belfast, UK

Published online: January 2006

DOI: 10.1038/npg.els.0005498

Most proteins undergo modification involving specific cleavage of the polypeptide backbone and/or changes to the side chains. Some of these modifications result in disease or disorder; others may be used diagnostically.

Keywords: posttranslational; processing; amyloid; glycosylation; toxins

Figure 1. Three major types of posttranslational modification. (1) Cleavage of the backbone by specific proteases (P). (2) Modifications of the side chains by the addition of a group (A) catalyzed by transferases and other enzymes (T); some of these are reversible by various hydrolases (H). (3) Nonenzymic modifications by reactive molecules, ions and radicals.
Figure 2. Metabolism of amyloid precursor protein (APP). The location of the A fragment is highlighted. (a) Action of and secretases. (b) Action of and secretases producing A (the amyloidogenic pathway).
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Related Sub-Topics:

Protein Structure | Protein Folding, Evolution and Degradation | Specific Genetic Disorders | Mutational Mechanisms of Genetic Disease | Posttranslational Modification
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Article Title: Posttranslational Modification and Human Disorders
 
How to Cite close
Wisdom, G Brian(Jan 2006) Posttranslational Modification and Human Disorders. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0005498]