IDPsBind

The 'IDPsBind' database is a resource that catalogs interaction sites between intrinsically disordered proteins (IDPs) and their binding ligands. IDPs lack a stable three-dimensional structure under physiological conditions but are involved in essential biological processes by interacting with other molecules. IDPsBind achieves this by utilizing the distance threshold method and mining 3D structural data from known IDPs complexes within the PDB database.
Key features of IDPsBind include:
- Inclusion of 9,626 IDPs complexes.
- Incorporation of 880 experimentally verified intrinsically disordered proteins.
- Providing comprehensive interaction sites within known 3D structures of IDPs complexes.

IDPsBind serves as a resource for researchers and scientists interested in the interaction mechanisms of IDPs and provides a foundation for developing algorithms that predict interaction sites within intrinsically disordered proteins.

Topic

Protein disordered structure;Small molecules;Protein binding sites;Physiology;Endocrinology and metabolism

Detail

  • Operation: Protein disorder prediction;Protein secondary structure prediction (coils);Protein-protein binding site prediction

  • Software interface: Web user interface

  • Language: -

  • License: -

  • Cost: Free

  • Version name: 1.0

  • Credit: The Special Project of the National Natural Science Foundation of China, the National Natural Science Foundation of China, the Scientific Research Program at Universities of Inner Mongolia Autonomous Region of China.

  • Input: -

  • Output: -

  • Contact: YongE Feng yefeng@imau.edu.cn

  • Collection: -

  • Maturity: -

Publications

  • IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures.
  • Sun C, et al. IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures. IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures. 2022; 23:33. doi: 10.1186/s12860-022-00434-5
  • https://doi.org/10.1186/S12860-022-00434-5
  • PMID: 35883018
  • PMC: PMC9327236

Download and documentation

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