ArticleThe Journal of biological chemistry2010
Intra- and interdomain effects due to mutation of calcium-binding sites in calmodulin.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Molecular basis for a CaThe Journal of biological chemistry · 2026Article
- Role of water-bridged interactions in metal ion coupled protein allostery.PLoS computational biology · 2022Article
- EF-hand protein, EfhP, specifically binds CaScientific reports · 2022Article
- The stress induced caleosin, RD20/CLO3, acts as a negative regulator of GPA1 in Arabidopsis.Plant molecular biology · 2021Article
- Article
- Non-Additive Effects of Binding Site Mutations in Calmodulin.Biochemistry · 2019Article
- Relative Cosolute Size Influences the Kinetics of Protein-Protein Interactions.Biophysical journal · 2015Article
- Two helices in the third intracellular loop determine anoctamin 1 (TMEM16A) activation by calcium.Pflugers Archiv : European journal of physiology · 2015Article
- Neurogranin alters the structure and calcium binding properties of calmodulin.The Journal of biological chemistry · 2014Article
- Surface dynamics in allosteric regulation of protein-protein interactions: modulation of calmodulin functions by Ca2+.PLoS computational biology · 2013Article
- The calmodulin regulator protein, PEP-19, sensitizes ATP-induced Ca2+ release.The Journal of biological chemistry · 2013Article
- The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.PLoS computational biology · 2011Article
- Intrinsically disordered PEP-19 confers unique dynamic properties to apo and calcium calmodulin.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The IQ-motif protein PEP-19, binds to the C-domain of calmodulin (CaM) with significantly different k(on) and k(off) rates in the presence and absence of Ca(2+), which could play a role in defining the levels of free CaM during Ca(2+) transients. The initial goal of the current study was to determine whether Ca(2+) binding to sites III or IV in the C-domain of CaM was responsible for affecting the kinetics of binding PEP-19. EF-hand Ca(2+)-binding sites were selectively inactivated by the common strategy of changing Asp to Ala at the X-coordination position. Although Ca(2+) binding to both sites III and IV appeared necessary for native-like interactions with PEP-19, the data also indicated that the mutations caused undesirable structural alterations as evidenced by significant changes in amide chemical shifts for apoCaM. Mutations in the C-domain also affected chemical shifts in the unmodified N-domain, and altered the Ca(2+) binding properties of the N-domain. Conversion of Asp(93) to Ala caused the greatest structural perturbations, possibly due to the loss of stabilizing hydrogen bonds between the side chain of Asp(93) and backbone amides in apo loop III. Thus, although these mutations inhibit binding of Ca(2+), the mutated CaM may not be able to support potentially important native-like activity of the apoprotein. This should be taken into account when designing CaM mutants for expression in cell culture.
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Registered trials
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