Protein Allostery and Sequence Design Principle
نویسندگان
چکیده
منابع مشابه
Protein Allostery and Conformational Dynamics.
The functions of many proteins are regulated through allostery, whereby effector binding at a distal site changes the functional activity (e.g., substrate binding affinity or catalytic efficiency) at the active site. Most allosteric studies have focused on thermodynamic properties, in particular, substrate binding affinity. Changes in substrate binding affinity by allosteric effectors have gene...
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Allosteric interactions between residues that are spatially apart and well separated in sequence are important in the function of multimeric proteins as well as single-domain proteins. This observation suggests that, among the residues that are involved in long-range communications, mutation at one site should affect interactions at a distant site. By adopting a sequence-based approach, we pres...
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The analysis of correlated sequence variation in evolutionarily related proteins is beginning to provide useful information regarding allosteric coupling between different functional sites. Such an analysis has been carried out for the nuclear hormone receptors, and the conclusions tested by making mutations that switch the allosteric response to ligands of RXR heterodimers.
متن کاملAllostery through protein-induced DNA bubbles
Allostery through DNA is increasingly recognized as an important modulator of DNA functions. Here, we show that the coalescence of protein-induced DNA bubbles can mediate allosteric interactions that drive protein aggregation. We propose that such allostery may regulate DNA's flexibility and the assembly of the transcription machinery. Mitochondrial transcription factor A (TFAM), a dual-functio...
متن کاملThe changing landscape of protein allostery.
It is becoming increasingly clear that the fundamental capacity to undergo conformational change in response to ligand binding is intrinsic to proteins. This property confers on proteins the ability to be allosterically modulated in order to shift substrate binding affinities, alter enzymatic activity or regulate protein-protein interaction. How this allosteric modulation occurs--the pathways o...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2012
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.52.150