Serdiuk I N
Mol Biol (Mosk). 2007 Mar-Apr;41(2):297-313.
The point of view that a uniquely folded protein tertiary structure is required for the protein functioning has been prevailing in the literature quite recently. However of lately it has been found that many proteins in a cell have no such structure in an isolated state, though they have a well-defined function in physiological conditions. These proteins were named as proteins with natural or internal disorder. The portion of disordered regions in such proteins may vary from a sequence of several amino acids to a completely disordered sequence containing from tens to hundreds of amino acids. The main difference of these proteins from the structured (globular) ones is that they have no unique tertiary structure in an isolated state and acquire it after interaction with their partners. Their conformation in such a complex depends on the interacting partner and not only on their own amino acid sequence, which is specific for structured (globular) proteins. The problem of structural and functional relations in the structured proteins and proteins with internal disorder is discussed in this review. The complexity of the problem and its potential solutions are illustrated by the example of elongation factors EFlA.
蛋白质发挥功能需要独特折叠的蛋白质三级结构这一观点，直到最近在文献中还一直占据主导地位。然而，最近发现细胞中的许多蛋白质在分离状态下并没有这种结构，尽管它们在生理条件下具有明确的功能。这些蛋白质被称为具有天然或内在无序的蛋白质。此类蛋白质中无序区域的部分长度可能从几个氨基酸序列到包含数十至数百个氨基酸的完全无序序列不等。这些蛋白质与结构化（球状）蛋白质的主要区别在于，它们在分离状态下没有独特的三级结构，而是在与它们的相互作用伙伴相互作用后才获得。它们在这样一个复合物中的构象取决于相互作用伙伴，而不仅仅取决于它们自身的氨基酸序列，而结构化（球状）蛋白质的构象则仅由其氨基酸序列决定。本文综述讨论了结构化蛋白质和具有内在无序的蛋白质的结构与功能关系问题。以延伸因子EFlA为例说明了该问题的复杂性及其潜在解决方案。
