Hot spots for allosteric regulation on protein surfaces.
Hot spots for allosteric regulation on protein surfaces.
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DOI:
10.1016/j.cell.2011.10.049
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发表时间:
2011-12-23
期刊:
影响因子:
64.5
通讯作者:
Ranganathan R
中科院分区:
文献类型:
--
作者:
Reynolds KA;McLaughlin RN;Ranganathan R
Recent work indicates a general architecture for proteins in which sparse networks of physically contiguous and co-evolving amino acids underlie basic aspects of structure and function. These networks, termed sectors, are spatially organized such that active sites are linked to many surface sites distributed throughout the structure. Using the metabolic enzyme dihydrofolate reductase as a model system, we show that (1) the sector is strongly correlated to a network of residues undergoing millisecond conformational fluctuations associated with enzyme catalysis and (2) sector-connected surface sites are statistically preferred locations for the emergence of allosteric control in vivo. Thus, sectors represent an evolutionarily conserved “wiring” mechanism that can enable perturbations at specific surface positions to rapidly initiate conformational control over protein function. These findings suggest that sectors enable the evolution of intermolecular communication and regulation.
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DOI:
10.1126/science.1198542
发表时间:
2011-04-08
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Bhabha G;Lee J;Ekiert DC;Gam J;Wilson IA;Dyson HJ;Benkovic SJ;Wright PE
通讯作者:
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影响因子:
9.8
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DOI:
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发表时间:
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期刊:
Science (New York, N.Y.)
影响因子:
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作者:
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影响因子:
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Wright, Peter E.
影响因子:
64.8
作者:
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