4.6 Article

Intrinsic protein disorder and conditional folding in AlphaFoldDB

期刊

PROTEIN SCIENCE
卷 31, 期 11, 页码 -

出版社

WILEY
DOI: 10.1002/pro.4466

关键词

CAID; critical assessment; intrinsically disordered proteins; machine learning; protein structure; structural bioinformatics

资金

  1. European Union's Horizon 2020
  2. Marie Sklodowska-Curie [778247]
  3. Italian Ministry of University and Research [2017483NH8]
  4. ELIXIR

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AlphaFoldDB provides a fresh perspective on predicting intrinsically disordered regions (IDRs) and conditionally folded binding regions, showing high competitiveness in these predictions and demonstrating the plasticity of the disorder to structure continuum.
Intrinsically disordered regions (IDRs) defying the traditional protein structure-function paradigm have been difficult to analyze. The availability of accurate structure predictions on a large scale in AlphaFoldDB offers a fresh perspective on IDR prediction. Here, we establish three baselines for IDR prediction from AlphaFoldDB models based on the recent CAID dataset. Surprisingly, AlphaFoldDB is highly competitive for predicting both IDRs and conditionally folded binding regions, demonstrating the plasticity of the disorder to structure continuum.

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