Extreme Fuzziness: Direct Interactions between Two IDPs

Biomolecules
Wenning Wang, Dongdong Wang

Abstract

Protein interactions involving intrinsically disordered proteins (IDPs) greatly extend the range of binding mechanisms available to proteins. In interactions employing coupled folding and binding, IDPs undergo disorder-to-order transitions to form a complex with a well-defined structure. In many other cases, IDPs retain structural plasticity in the final complexes, which have been defined as the fuzzy complexes. While a large number of fuzzy complexes have been characterized with variety of fuzzy patterns, many of the interactions are between an IDP and a structured protein. Thus, whether two IDPs can interact directly to form a fuzzy complex without disorder-to-order transition remains an open question. Recently, two studies of interactions between IDPs (4.1G-CTD/NuMA and H1/ProTα) have found a definite answer to this question. Detailed characterizations combined with nuclear magnetic resonance (NMR), single-molecule Förster resonance energy transfer (smFRET) and molecular dynamics (MD) simulation demonstrate that direct interactions between these two pairs of IDPs do form fuzzy complexes while retaining the conformational dynamics of the isolated proteins, which we name as the extremely fuzzy complexes. Extreme fuzziness comp...Continue Reading

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Citations

Apr 14, 2019·Biomolecules·Prakash Kulkarni, Vladimir N Uversky
Dec 24, 2020·Physical Chemistry Chemical Physics : PCCP·Wenning Wang
Jul 22, 2021·Computational and Structural Biotechnology Journal·Ilinka ClercJuan Cortés

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Methods Mentioned

BETA
NMR
circular dichroism
FRET
fluorescence correlation spectroscopy
protein folding

Software Mentioned

Frustratometer
NuMA

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