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Protein recognition and disorder: A debate
Date:1/11/2013

The extent to which three-dimensional structure is required for protein recognition and function is an area of vigorous debate with clear implications for protein engineering. Two differing viewpoints have been put forward in two articles published in F1000 Biology Reports today.

In structuring their arguments, the authors were encouraged to consider the opposing viewpoint, examine the points put forward and critique them in their own articles. This novel collaborative approach has given rise to a considered exchange of ideas and may consequently stimulate further research in the field.

In their article entitled "The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure", Keith Dunker (Indiana University School of Medicine) and Vladimir N. Uversky (Russian Academy of Sciences and University of South Florida) argue that the lock and key model of protein recognition cannot be upheld as a universal truth. They argue that some proteins without a rigid structure, intrinsically disordered proteins (IDPs), still have function.

In contrast, Jol Janin (Universit Paris-Sud) and Michael J.E. Sternberg (Imperial College, London), in their article "Protein flexibility, not disorder, is intrinsic to molecular recognition", argue that a protein's function in the real world environment of the body's cells is dependent on the structure of that protein, and that protein recognition requires regions of complementary structure binding to each other. Janin and Sternberg also note that many proteins seem to be disordered in the test tube but are in fact proteins waiting for partners (PWPs), which then adopt fully ordered structures in the presence of other components of the cell required to perform a function.

To counter the argument pu
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Contact: Eleanor Howell
press@f1000.com
44-020-763-19129
Faculty of 1000: Biology and Medicine
Source:Eurekalert

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