Structural Changes beyond the EF-Hand Contribute to Apparent Calcium Binding Affinities: Insights from Parvalbumins.

ABSTRACT: Members of the parvalbumin (PV) family of calcium (Ca²⁺) binding proteins (CBPs) share a relatively high level of sequence similarity. However, their Ca²⁺ affinities and selectivities against competing ions like Mg²⁺ can widely vary. We conducted molecular dynamics simulations of several α-parvalbumin (αPV) constructs with micromolar to nanomolar Ca²⁺ affinities to identify structural and dynamic features that contribute to their binding of ions. Specifically, we examined a D94S/G98E construct with a lower Ca²⁺ affinity (≈-18 kcal/mol) relative to the wild type (WT) (≈-22 kcal/mol) and an S55D/E59D variant with enhanced affinity (≈-24 kcal/mol). Additionally, we also examined the binding of Mg²⁺ to these isoforms, which is m

SUBMITTER: Immadisetty K 

PROVIDER: S-EPMC8848088 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature