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Do calmodulin binding IQ motifs have built‐in capping domains?
Author(s) -
MuguruzaMontero Arantza,
Ramis Rafael,
Nuñez Eider,
R. Ballesteros Oscar,
G. Ibarluzea Markel,
Araujo Ariane,
MAlicante Sara,
Urrutia Janire,
Leonardo Aritz,
Bergara Aitor,
Villarroel Alvaro
Publication year - 2021
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.4170
Subject(s) - calmodulin , docking (animal) , binding site , structural motif , computational biology , structural similarity , chemistry , helix (gastropod) , motif (music) , common core , biophysics , biology , genetics , crystallography , core (optical fiber) , biochemistry , computer science , physics , medicine , snail , ecology , nursing , acoustics , enzyme , telecommunications
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.