Thermodynamics of Multiple Molecular Recognition by Intrinsically Disordered Protein

生物系统中产生的蛋白质具有明确的结构以获得其独特的功能。然而，有许多内在无序蛋白（IDPs）在基因组序列中不能自己形成特定的结构。IDPs在与特定配体结合后形成有序的结构。本研究分析了肠出血性大肠杆菌病原菌EspB与配体结合的理化机制。我们发现EspB通过在G41-E70周围形成的不稳定的α -螺旋区以“构象选择”的方式与α -catenin结合。

Proteins produced in biological systems assume well-defined structures to obtain their unique functions. However, there are many intrinsically disordered proteins (IDPs) which are unable to form specific structures by themselves in genomic sequences. IDPs form well-ordered structures upon binding to their specific ligands.Here, we analysed physicochemical mechanism of ligand binding by EspB, an IDP pathogens from enterohaemorrhagic E. coli. We found that EspB binds to alpha-catenin through the unstable alpha-helical regions formed around G41-E70 in a manner of "Conformational Selection".