The sequence-ensemble relationship in fuzzy protein complexes.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
14 09 2021
Historique:
accepted: 11 06 2021
entrez: 10 9 2021
pubmed: 11 9 2021
medline: 15 12 2021
Statut: ppublish

Résumé

Intrinsically disordered proteins (IDPs) interact with globular proteins through a variety of mechanisms, resulting in the structurally heterogeneous ensembles known as fuzzy complexes. While there exists a reasonable comprehension on how IDP sequence determines the unbound IDP ensemble, little is known about what shapes the structural characteristics of IDPs bound to their targets. Using a statistical thermodynamic model, we show that the target-bound ensembles are determined by a simple code that combines the IDP sequence and the distribution of IDP-target interaction hotspots. These two parameters define the conformational space of target-bound IDPs and rationalize the observed structural heterogeneity of fuzzy complexes. The presented model successfully reproduces the dynamical signatures of target-bound IDPs from the NMR relaxation experiments as well as the changes of interaction affinity and the IDP helicity induced by mutations. The model explains how the target-bound IDP ensemble adapts to mutations in order to achieve an optimal balance between conformational freedom and interaction energy. Taken together, the presented sequence-ensemble relationship of fuzzy complexes explains the different manifestations of IDP disorder in folding-upon-binding processes.

Identifiants

pubmed: 34504009
pii: 2020562118
doi: 10.1073/pnas.2020562118
pmc: PMC8449401
pii:
doi:

Substances chimiques

Intrinsically Disordered Proteins 0
Ligands 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

San Hadži (S)

Department of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia; san.hadzi@fkkt.uni-lj.si jurij.lah@fkkt.uni-lj.si.
Department of Synthetic Biology and Immunology, National Institute of Chemistry, SI-1000 Ljubljana, Slovenia.

Remy Loris (R)

Structural Biology Brussels, Department of Biotechnology, Vrije Universiteit Brussel, 1050 Brussels, Belgium.
Center for Structural Biology, Vlaams Instituut voor Biotechnologie, 1050 Brussels, Belgium.

Jurij Lah (J)

Department of Physical Chemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia; san.hadzi@fkkt.uni-lj.si jurij.lah@fkkt.uni-lj.si.

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Classifications MeSH