Intrinsic disorder in proteins resulting in considerable variation in structure can lead to multiple functions including multi-specificity and diverse pathologies. Protein interfaces can involve disordered regions that assemble through a concerted-fold-and-bind mechanism. The binding involves both enthalpic and entropic gains by exploiting ‘hot spots’ on the partner and displacing water molecules placed in thermodynamically unfavorable situations. The examples of Rad51-BRCA2 and Artemis-DNA-PKCs/LigIV complexes illustrate this in the context of drug design. This overview tracks the seamless involvement of protein disorder in multi-specificity of biocatalysts, protein assembly formations and host-pathogen interactions, where intrinsic disorder can in Mycobacteria, compensate for genome reduction by carrying out multiple functions and in some RNA viruses facilitate adaption to the host. These present challenging opportunities for designing new drugs and interventions.

蛋白质的内在失调导致结构上的显着变化，可导致多种功能，包括多特异性和多种病理。蛋白质界面可能涉及通过协调折叠和结合机制组装的无序区域。通过利用配偶体上的“热点”并置换处于热力学不利条件下的水分子，这种结合既包括焓增也包括熵增。Rad51-BRCA2和Artemis-DNA-PKCs / LigIV复合物的例子在药物设计的背景下说明了这一点。本概述跟踪了蛋白质疾病与生物催化剂，蛋白质装配体形成和宿主-病原体相互作用的多特异性之间的无缝关联，而固有疾病可以在分枝杆菌中发生，通过执行多种功能来补偿基因组的减少，并且在某些RNA病毒中有助于适应宿主。这些为设计新药和干预措施带来了挑战性的机遇。