English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Intrinsically disordered proteins (IDPs) and proteins with intrinsicallydisordered regions (IDRs) govern a daunting number of physiological processes.For such proteins, molecular mechanisms governing their interactions withproteins involved in signal transduction pathways remain unclear. Using thefolded, calcium-loaded calmodulin (CaM) interaction with the calcineurinregulatory IDP as a prototype for IDP-mediated signal transduction events, weuncover the interplay of IDP structure and electrostatic interactions indetermining the kinetics of protein-protein association. Using an array ofbiophysical approaches including stopped-flow and computational simulation, wequantify the relative contributions of electrostatic interactions andconformational ensemble characteristics in determining association kinetics ofcalmodulin (CaM) and the calcineurin regulatory domain (CaN RD). Our chieffindings are that CaM/CN RD association rates are strongly dependent on ionicstrength and that observed rates are largely determined by theelectrostatically-driven interaction strength between CaM and the narrow CaN RDcalmodulin recognition domain. These studies highlight a molecular mechanism ofcontrolling signal transduction kinetics that may be utilized in wide-rangingsignaling cascades that involve IDPs.

Electrostatic Forces Mediate Fast Association of Calmodulin and the Intrinsically Disordered Regulatory Domain of Calcineurin