TY - JOUR
T1 - Allostery
T2 - Absence of a Change in Shape Does Not Imply that Allostery Is Not at Play
AU - Tsai, Chung Jung
AU - del Sol, Antonio
AU - Nussinov, Ruth
N1 - Funding Information:
This project has been funded in whole or in part with Federal funds from the National Cancer Institute, National Institutes of Health, under contract number NO1-CO-12400. 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. This research was supported (in part) by the Intramural Research Program of the National Institutes of Health, National Cancer Institute, Center for Cancer Research.
PY - 2008/4/18
Y1 - 2008/4/18
N2 - Allostery is essential for controlled catalysis, signal transmission, receptor trafficking, turning genes on and off, and apoptosis. It governs the organism's response to environmental and metabolic cues, dictating transient partner interactions in the cellular network. Textbooks taught us that allostery is a change of shape at one site on the protein surface brought about by ligand binding to another. For several years, it has been broadly accepted that the change of shape is not induced; rather, it is observed simply because a larger protein population presents it. Current data indicate that while side chains can reorient and rewire, allostery may not even involve a change of (backbone) shape. Assuming that the enthalpy change does not reverse the free-energy change due to the change in entropy, entropy is mainly responsible for binding.
AB - Allostery is essential for controlled catalysis, signal transmission, receptor trafficking, turning genes on and off, and apoptosis. It governs the organism's response to environmental and metabolic cues, dictating transient partner interactions in the cellular network. Textbooks taught us that allostery is a change of shape at one site on the protein surface brought about by ligand binding to another. For several years, it has been broadly accepted that the change of shape is not induced; rather, it is observed simply because a larger protein population presents it. Current data indicate that while side chains can reorient and rewire, allostery may not even involve a change of (backbone) shape. Assuming that the enthalpy change does not reverse the free-energy change due to the change in entropy, entropy is mainly responsible for binding.
KW - entropy
KW - network
KW - residue communication
KW - rewiring
KW - thermodynamics
UR - http://www.scopus.com/inward/record.url?scp=41149104308&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2008.02.034
DO - 10.1016/j.jmb.2008.02.034
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AN - SCOPUS:41149104308
SN - 0022-2836
VL - 378
SP - 1
EP - 11
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 1
ER -