PulseTrendingJournal ClubResearchersJournalsExplore
Instagram
HomeTrendingJournal ClubExplore
Synapse
⌘+K
Synapse
May 17, 2026Journal of Structural Biology XOpen Access

Structural insights into interdomain interactions in Entamoeba histolytica APS kinase

View Full Paper
Ask AI
Bookmark
Share

Authors

RHRyo HatanakaYOYukiko OhsumiHMHiroki Matsui

Discussion

Loading...

Member takes

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
View Full Paper
Ask AI
Bookmark
Share