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. 2018 Dec 17;9:1484. doi: 10.3389/fphar.2018.01484

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Copyright © 2018 Hendrickx, van Gastel, Leysen, Santos-Otte, Premont, Martin and Maudsley.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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A graphical block depiction (A) of the multiple functional regions of human GRK5 indicates the diverse range of activities mediated by this protein (α-N, terminal domain; PIP2, phosphatidylinositol bisphosphate binding domain; RH, Regulator of G protein signaling homology domain; NES, Nuclear Export Sequence; NLS, Nuclear Localization Sequence). In the primary sequence two autophosphorylation sites are indicated within the catalytic domain. A crystal-assisted model of human GRK5 (B) was constructed and annotated using 3DBionotes-WS (http://3dbionotes.cnb.csic.es/ws). This model indicates the three-dimensional proximities of the α-N domain (green), PIP2 binding domains (blue), NES (pink), catalytic domain (orange), and the NLS domain (red).