Protein flexibility, not disorder, is intrinsic to molecular recognition.

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Title: Protein flexibility, not disorder, is intrinsic to molecular recognition.
Author(s): Janin, J
Sternberg, MJE
Item Type: Journal Article
Abstract: An 'intrinsically disordered protein' (IDP) is assumed to be unfolded in the cell and perform its biological function in that state. We contend that most intrinsically disordered proteins are in fact proteins waiting for a partner (PWPs), parts of a multi-component complex that do not fold correctly in the absence of other components. Flexibility, not disorder, is an intrinsic property of proteins, exemplified by X-ray structures of many enzymes and protein-protein complexes. Disorder is often observed with purified proteins in vitro and sometimes also in crystals, where it is difficult to distinguish from flexibility. In the crowded environment of the cell, disorder is not compatible with the known mechanisms of protein-protein recognition, and, foremost, with its specificity. The self-assembly of multi-component complexes may, nevertheless, involve the specific recognition of nascent polypeptide chains that are incompletely folded, but then disorder is transient, and it must remain under the control of molecular chaperones and of the quality control apparatus that obviates the toxic effects it can have on the cell.
Publication Date: 11-Jan-2013
URI: http://hdl.handle.net/10044/1/56808
DOI: https://dx.doi.org/10.3410/B5-2
ISSN: 1757-594X
Start Page: 2
Journal / Book Title: F1000 Biol Rep
Volume: 5
Copyright Statement: This is an open-access article distributed under the terms of the Creative Commons Attribution-Non Commercial License (http://creativecommons.org/licenses/by-nc/3.0/legalcode), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. You may not use this work for commercial purposes. The electronic version of this article is the complete one and can be found at: http://f1000.com/prime/reports/b/5/2
Publication Status: Published
Conference Place: England
Appears in Collections:Faculty of Natural Sciences



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