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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Uversky, Vladimir N. |
| Description | Author Affiliation: Uversky VN ( Department of Molecular Medicine, University of South Florida, Tampa, FL, USA. vuversky@health.usf.edu) |
| Abstract | Intrinsically disordered proteins are highly abundant in nature and play a number of crucial roles in the living cells. They are commonly involved in a wide range of intermolecular interactions, and some of them possess remarkable binding promiscuity, being able to interact specifically with structurally unrelated partners. Although they do not have well-folded structure, some IDPs are known to fold at binding to their specific partners. IDPs are highly pliable and one IDP can form an array of unrelated structures being bound to different partners. It is believed that many IDPs, being mostly disordered, have transient elements of the preformed secondary structure which are highly interaction prone and is used by IDPs for binding to specific partners. The overall disordered nature of IDPs, their high conformational dynamics and flexibility, the presence of sticky preformed binding elements, and their ability to morph into differently-shaped bound configurations raised a very important question about the mechanisms preventing IDPs from unwanted interactions with non-native partners. In this review, a concept of functional misfolding is introduced. Accumulated to date data on the conformational behavior and fine structure of several IDPs suggest that the preformed binding elements might be involved in a set of non-native intramolecular interactions. In other words, there is a chance that a polypeptide chain misfolds to sequester the preformed elements inside the non-interactive or less-interactive cage, therefore preventing these elements from the unnecessary and unwanted interactions with non-native binding partners. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 5 |
| Volume Number | 1814 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2011-05-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Proteins Chemistry Metabolism Models, Molecular Protein Binding Protein Folding Protein Structure, Secondary Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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