Journal
BIOCHIMIE
Volume 89, Issue 3, Pages 419-421Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2006.11.003
Keywords
NMR; dimerization; intrinsically unstructured proteins; protein-protein interactions
Categories
Funding
- NIAID NIH HHS [P30 AI042845, P30 AI042845-08, P30 AI42845-08] Funding Source: Medline
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There are a large number of protein domains and even entire proteins, lacking ordered structure under physiological conditions. Intriguingly, a highly flexible, random coil-like conformation is the native and functional state for many proteins known to be involved in cell signaling. An example is a key component of immune signaling, the cytoplasmic region of the T cell receptor subunit. This domain exhibits specific dimerization that is distinct from non-specific aggregation behavior seen in many systems. In this work, we use diffusion and chemical shift mapping NMR data to show that the protein does not undergo a transition between disordered and ordered states upon dimerization. This finding opposes the generally accepted view on the behavior of intrinsically disordered proteins, provides evidence for the existence of specific dimerization interactions for intrinsically disordered protein species and opens a new line of research in this new and quickly developing field. (c) 2006 Elsevier Masson SAS. All rights reserved.
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