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Structure-based classification of 45 FK506-binding proteins.

J A Somarelli1, S Y Lee, J Skolnick

  • 1Department of Biological Sciences, OE304, Florida International University, Miami, Florida 33199, USA.

Proteins
|January 25, 2008
PubMed
Summary
This summary is machine-generated.

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FK506-binding proteins (FKBPs) are crucial chaperones with diverse roles. Computational modeling revealed evolutionary changes and potential new functions, including drug interactions and nucleic acid binding.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • FK506-binding proteins (FKBPs) are conserved chaperones involved in numerous cellular processes.
  • Their functions are linked to specific tertiary structures and domains.
  • Understanding FKBP structure-function relationships is key to deciphering their roles.

Purpose of the Study:

  • To predict and analyze the tertiary structures of a diverse set of FKBP proteins.
  • To classify FKBP homologs based on structural predictions.
  • To investigate potential evolutionary modifications and novel functional interactions of FKBPs.

Main Methods:

  • Tertiary structure prediction using the Threading/ASSEmbly/Refinement (TASSER) approach for 45 FKBP proteins across 23 species.

Related Experiment Videos

  • Comparison of predicted models with existing FKBP solution structures.
  • Identification of homologous protein groups and evolutionary sequence modifications.
  • Molecular docking simulations to explore drug binding and protein-protein interactions.

    • Main Results:

    • Successfully predicted tertiary structures for 45 FKBP proteins, enabling homology-based classification.
    • Identified significant evolutionary modifications within the FKBP family, including domain losses, duplications, and motif insertions.
    • Docking simulations suggested that extrachain segments influence drug binding affinity.
    • Revealed a potential helix-loop-helix (HLH) region in some FKBPs, implicating them in nucleic acid interactions.

    Conclusions:

    • The structural classification of FKBPs aids in inferring functions of newly identified members.
    • FKBP evolution involves substantial structural diversification.
    • FKBPs possess uncharacterized regions and domains that influence their interactions with drugs and nucleic acids, expanding their known functional repertoire.