Allostery: Absence of a change in shape does not imply that allostery is not at play

被引：368

作者：

Tsai, Chung-Jung ^{[1
]}

del Sol, Antonio ^{[2
]}

Nussinov, Ruth ^{[1
,3
]}

机构：

[1] NCI, Ctr Canc Res Nanobiol, SAIC Frederick, Basic Res Program, Frederick, MD 21702 USA

[2] Fujirebio Inc, Div Res & Dev, Bioinformat Res Unit, Hachioji, Tokyo 1920031, Japan

[3] Tel Aviv Univ, Sackler Sch Med, Dept Human Genet & Mol Med, Sackler Inst Mol Med, IL-69978 Tel Aviv, Israel

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2008年 / 378卷 / 01期

关键词：

residue communication; thermodynamics; entropy; network; rewiring;

D O I：

10.1016/j.jmb.2008.02.034

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1 / 11

页数：11

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