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PEP-19 modulates calcium binding to calmodulin by electrostatic steering

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  • Xu Wang

    (McGovern Medical at UTHealth, 6431 Fannin)

  • John A. Putkey

    (McGovern Medical at UTHealth, 6431 Fannin)

Abstract

PEP-19 is a small protein that increases the rates of Ca2+ binding to the C-domain of calmodulin (CaM) by an unknown mechanism. Although an IQ motif promotes binding to CaM, an acidic sequence in PEP-19 is required to modulate Ca2+ binding and to sensitize HeLa cells to ATP-induced Ca2+ release. Here, we report the NMR solution structure of a complex between PEP-19 and the C-domain of apo CaM. The acidic sequence of PEP-19 associates between helices E and F of CaM via hydrophobic interactions. This allows the acidic side chains in PEP-19 to extend toward the solvent and form a negatively charged surface that resembles a catcher’s mitt near Ca2+ binding loop III of CaM. The topology and gradients of negative electrostatic surface potential support a mechanism by which PEP-19 increases the rate of Ca2+ binding to the C-domain of CaM by ‘catching’ and electrostatically steering Ca2+ to site III.

Suggested Citation

  • Xu Wang & John A. Putkey, 2016. "PEP-19 modulates calcium binding to calmodulin by electrostatic steering," Nature Communications, Nature, vol. 7(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13583
    DOI: 10.1038/ncomms13583
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