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. 2024 Apr 19;22:233. doi: 10.1186/s12964-024-01612-y

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — ColabFold 5-HT7R/CDK5 interaction interface prediction and comparison to CDK5/p25 complex. A General view of energy minimized ColabFold model for m5-HT7R/CDK5 protein complex. Enlarged view shows of contacts between ICL3 and CDK5 αC-helix. 5-HT7R is shown in orange and CDK5 in light cyan color. B Scheme depicts amino acid residues within m5-HT7R ICL3 and CDK5 αC-helix proposed to be involved in m5-HT7R/CDK5 interaction interface. C. Scheme depicts amino acid residues within α5 and α6 p25 domains and CDK5 αC-helix involved in formation of interaction interface (based on X-ray crystal structure 1H4L [53]. The α-helixes are shown as ovals and β-sheets as parallelograms. The CDK5 PSSALRE region is highlighted as a violet helix. Images in (B) and (C) were created using BioRender