ReviewProtein science : a publication of the Protein Society2021
Do calmodulin binding IQ motifs have built-in capping domains?
Review in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Genome-Wide Identification and Expression Pattern of theInternational journal of molecular sciences · 2026Article
- Calmodulin assists during co-translational folding of the KProtein science : a publication of the Protein Society · 2026Article
- The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026Article
- Do calmodulin binding IQ motifs have built-in capping domains?Protein science : a publication of the Protein Society · 2021Review
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11 authors.
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Abstract
Most calmodulin (CaM) targets are α-helices. It is not clear if CaM induces the adoption of an α-helix configuration to its targets or if those targets are selected as they spontaneously adopt an α-helical conformation. Other than an α-helix propensity, there is a great variety of CaM targets with little more in common. One exception to this rule is the IQ site that can be recognized in a number of targets, such as those ion channels belonging to the KCNQ family. Although there is negligible sequence similarity between the IQ motif and the docking site on SK2 channels, both adopt a similar three-dimensional disposition. The isolated SK2 target presents a pre-folded core region that becomes fully α-helical upon binding to CaM. The existence of this pre-folded state suggests the occurrence of capping within CaM targets. In this review, we examine the capping properties within the residues flanking this core domain, and relate known IQ motifs and capping.
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