TY - JOUR

T1 - Order/Disorder Transitions Upon Protein Binding: A Unifying Perspective

AU - Lebedenko, Olga O.

AU - Sekhar, Ashok

AU - Скрынников, Николай Русланович

N1 - eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.26737

PY - 2024/12/1

Y1 - 2024/12/1

N2 - When two proteins bind to each other, this process is often accompanied by a change in their structural states (from disordered to ordered or vice versa). As it turns out, there are 10 distinct possibilities for such binding-related order/disorder transitions. Out of this number, seven scenarios have been experimentally observed, while another three remain hitherto unreported. As an example, we discuss the so-called mutual synergistic folding, whereby two disordered proteins come together to form a fully structured complex. Our bioinformatics analysis of the Protein Databank found potential new examples of this remarkable binding mechanism.

AB - When two proteins bind to each other, this process is often accompanied by a change in their structural states (from disordered to ordered or vice versa). As it turns out, there are 10 distinct possibilities for such binding-related order/disorder transitions. Out of this number, seven scenarios have been experimentally observed, while another three remain hitherto unreported. As an example, we discuss the so-called mutual synergistic folding, whereby two disordered proteins come together to form a fully structured complex. Our bioinformatics analysis of the Protein Databank found potential new examples of this remarkable binding mechanism.

KW - HsCen2–XPC complex

KW - mutual synergistic folding

KW - protein (un)folding coupled to binding

KW - ZNHIT3–NUFIP1 complex

UR - https://www.mendeley.com/catalogue/1ac765eb-79fd-30be-bcb2-6f39bcfee981/

U2 - 10.1002/prot.26737

DO - 10.1002/prot.26737

M3 - Article

VL - 92

SP - 1459

EP - 1463

JO - Proteins: Structure, Function and Bioinformatics

JF - Proteins: Structure, Function and Bioinformatics

SN - 0887-3585

IS - 12

ER -