{
  "id": 16701478,
  "title": "A structural screen for candidate polyphosphate binding surfaces in human membrane associated proteins",
  "url": "https://urgent.news/2026/10/26/a-structural-screen-for-candidate-polyphosphate-binding-surfaces-in",
  "topic": "science",
  "section": "Science",
  "published": "2026-10-26T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.10.25.761654v1?rss=1"
  },
  "original_language": "en",
  "account": null,
  "summary": "Inorganic polyphosphate (polyP) can alter protein function through noncovalent binding, yet its partners among human membrane associated proteins remain poorly characterized. PolyP is recognized through two modes: a structure-based mode driven by charge complementarity with sites assembled by protein folding, and a more recently defined sequence-based mode at histidine and lysine rich tracts. The…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}