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CDB-a database for protein heterodimeric complexes.

Malka Aker1, Shirly Ohanona1, Shira Fisher1

  • 1Department of Bioinformatics, Jerusalem College of Technology, 21 Havaad Haleumi Street, Jerusalem, Israel.

Protein Engineering, Design & Selection : PEDS
|November 20, 2018
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Summary
This summary is machine-generated.

The Complex DataBase (CDB) provides crystallographic structures for heterodimeric protein complexes and individual proteins. This resource aids in developing protein-protein interaction prediction methods and protein binding studies.

Keywords:
crystallographyprotein complex interactionsprotein dimersprotein–protein interfacestructure

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Area of Science:

  • Structural Biology
  • Proteomics
  • Bioinformatics

Background:

  • Crystallographic structures of protein complexes are crucial for advancing proteomic and structural biology.
  • These structures are vital for predicting protein-protein interaction (PPI) sites and protein-protein docking.
  • They also support the development of protein complexation inhibitors.

Purpose of the Study:

  • To introduce the Complex DataBase (CDB), a web application for accessing crystallographic structures of heterodimeric protein complexes.
  • To provide structures of individual unbound proteins alongside their complexed forms.
  • To facilitate research in protein binding studies and the development of PPI prediction methods.

Main Methods:

  • Development of a database web application (CDB).
  • Collection and curation of crystallographic structures of heterodimeric protein complexes.
  • Inclusion of individual unbound protein structures.
  • Provision of annotations for accessed structures.

Main Results:

  • The CDB offers direct access to crystallographic structures of protein complexes.
  • It includes structures of individual unbound proteins.
  • The database provides annotations to aid further research.

Conclusions:

  • The CDB serves as a valuable starting point for creating new experimental protein complex sets.
  • It supports protein binding studies and the development/evaluation of PPI prediction methods.
  • Access to curated structural data enhances research in structural biology and proteomics.