May 26, 2014

Supertertiary protein structure affects an allosteric network

BioRxiv : the Preprint Server for Biology
Nikolai SlavovAlexander van Oudenaarden

Abstract

The notion that protein function is allosterically regulated by structural or dynamic changes in proteins has been extensively investigated in several protein domains in isolation. In particular, PDZ domains have represented a paradigm for these studies, despite providing conflicting results. Furthermore, it is still unknown how the association between protein domains in supramodules, consitituting so-called supertertiary structure, affects allosteric networks. Here, we experimentally mapped the allosteric network in a PDZ:ligand complex, both in isolation and in the context of a supramodular structure, and show that allosteric networks in a PDZ domain are highly dependent on the supertertiary structure in which they are present. This striking sensitivity of allosteric networks to presence of adjacent protein domains is likely a common property of supertertiary structures in proteins. Our findings have general implications for prediction of allosteric networks from primary and tertiary structure and for quantitative descriptions of allostery.

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Mentioned in this Paper

Polyribosomes
Set of Polysomal Ribosomes
Ribosomal Proteins
Regulation of Biological Process
Yeasts
Protein Biosynthesis
RpIII toxin (Radianthus)
Mass Spectrometry
Mouse Embryonic Stem Cells
Ribosomes

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