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May 17, 2026Journal of Structural Biology X0 citationsOpen Access

Structural Insights Into Interdomain Interactions in Entamoeba histolytica APS Kinase

Structural insights into interdomain interactions in Entamoeba histolytica APS kinase

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Authors

RHRyo HatanakaYOYukiko OhsumiHMHiroki Matsui

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Overview

Randomized trial uncovers new regulatory mechanisms in Entamoeba histolytica APS kinase, suggesting evolutionary adaptations.

Key Points

  • The study aims to elucidate interdomain interactions within E. histolytica APS kinase and their functional implications.
  • Determined crystal structure of full-length APS kinase at 2.60 Å and truncated variant at 2.10 Å resolution.
  • Conducted x-ray crystallography and single-particle cryo-EM for structural insights.
  • Performed activity assays on mutants to explore regulatory mechanisms.
  • Characterized interdomain interactions that were not reported in other organisms.
  • Identified that the additional AS-like domain significantly influences the catalytic activity of APS kinase.
  • Proposed a novel regulatory mechanism involving transient interdomain contacts that modulate kinase activity.

Cite This Study

Hatanaka et al. (2026) studied this question.

synapsesocial.com/papers/6a095c147880e6d24efe206dhttps://doi.org/10.1016/j.yjsbx.2026.100147
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