Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt


  • Fulltext

    Forlagets udgivne version, 1,21 MB, PDF-dokument

Motifs within proteins help us categorize their functions. Intrinsically disordered proteins (IDPs) are rich in short linear motifs, conferring them many different roles. IDPs are also frequently highly charged and, therefore, likely to interact with ions. Canonical calcium-binding motifs, such as the EF-hand, often rely on the formation of stabilizing flanking helices, which are a key characteristic of folded proteins, but are absent in IDPs. In this study, we probe the existence of a calcium-binding motif relevant to IDPs. Upon screening several carefully selected IDPs using NMR spectroscopy supplemented with affinity quantification by colorimetric assays, we found calcium-binding motifs in IDPs which could be categorized into at least two groups—an Excalibur-like motif, sequentially similar to the EF-hand loop, and a condensed-charge motif carrying repetitive negative charges. The motifs show an affinity for calcium typically in the ~100 µM range relevant to regulatory functions and, while calcium binding to the condensed-charge motif had little effect on the overall compaction of the IDP chain, calcium binding to Excalibur-like motifs resulted in changes in compaction. Thus, calcium binding to IDPs may serve various structural and functional roles that have previously been underreported.

Udgave nummer8
Antal sider17
StatusUdgivet - 2021

Bibliografisk note

Funding Information:
Funding: This research was funded by the Novo Nordisk Foundation Challenge Grant REPIN (#NNF18OC0033926 to B.B.K. and K.S.) and by the Lundbeck Foundation BRAINSTRUC Structural Biology Initiative (R155-2015-2666) (K.L.L., A.E.L. and B.B.K.). All NMR data were recorded at cOpenNMR, an infrastructure facility funded by the Novo Nordisk Foundation (#NNF18OC0032996).

Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Antal downloads er baseret på statistik fra Google Scholar og

Ingen data tilgængelig

ID: 279622658