TY - JOUR
T1 - Induced fit, conformational selection and independent dynamic segments
T2 - An extended view of binding events
AU - Csermely, Peter
AU - Palotai, Robin
AU - Nussinov, Ruth
N1 - Funding Information:
The authors thank the anonymous referees for their helpful suggestions and we thank Mark Bathe and Do-Nyun Kim (Massachusetts Institute of Technology, Cambridge, MA), as well as Zaida Luthey-Shulten and John Eargle (University of Illinois at Urbana-Champaign, Urbana IL) for the images in Figure 2 . P.C. thanks Francesco Piazza (University of Portsmouth, UK), Yves-Henri Sanejouand (University of Nantes, France) and Gábor Simkó (Semmelweis University, Budapest, Hungary) for helpful discussions. Funding has been provided by the EU (FP6-518230) and by the Hungarian National Science Foundation (OTKA K69105). This project has been funded, in part, with federal funds from the National Cancer Institute, National Institutes of Health, under contract HHSN261200800001E. This research was supported, in part, by the Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products or organizations imply endorsement by the U.S. Government.
PY - 2010/10
Y1 - 2010/10
N2 - Single molecule and NMR measurements of protein dynamics increasingly uncover the complexity of binding scenarios. Here, we describe an extended conformational selection model that embraces a repertoire of selection and adjustment processes. Induced fit can be viewed as a subset of this repertoire, whose contribution is affected by the bond types stabilizing the interaction and the differences between the interacting partners. We argue that protein segments whose dynamics are distinct from the rest of the protein ('discrete breathers') can govern conformational transitions and allosteric propagation that accompany binding processes and, as such, might be more sensitive to mutational events. Additionally, we highlight the dynamic complexity of binding scenarios as they relate to events such as aggregation and signalling, and the crowded cellular environment.
AB - Single molecule and NMR measurements of protein dynamics increasingly uncover the complexity of binding scenarios. Here, we describe an extended conformational selection model that embraces a repertoire of selection and adjustment processes. Induced fit can be viewed as a subset of this repertoire, whose contribution is affected by the bond types stabilizing the interaction and the differences between the interacting partners. We argue that protein segments whose dynamics are distinct from the rest of the protein ('discrete breathers') can govern conformational transitions and allosteric propagation that accompany binding processes and, as such, might be more sensitive to mutational events. Additionally, we highlight the dynamic complexity of binding scenarios as they relate to events such as aggregation and signalling, and the crowded cellular environment.
UR - http://www.scopus.com/inward/record.url?scp=77957231785&partnerID=8YFLogxK
U2 - 10.1016/j.tibs.2010.04.009
DO - 10.1016/j.tibs.2010.04.009
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AN - SCOPUS:77957231785
VL - 35
SP - 539
EP - 546
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
SN - 0376-5067
IS - 10
ER -