Structures of immunophilins and their ligand complexes

Curr Top Med Chem. 2003;3(12):1392-409. doi: 10.2174/1568026033451899.

Abstract

This review includes an analysis of available X-ray and NMR structures of both members of the immunophilin family; cyclophilins and the FK-506 binding proteins (FKBPs). Available structures are compared and contrasted to highlight different structural features seen both within and between species. Each immunophilin family has been structurally characterised with a variety of small molecule ligands, principally immunosuppressive drugs and their analogues and an overview of these complexes is also presented. Currently the Protein Data Base contains over 60 entries for cyclophilins and over 40 entries for FKBPs. A number of FKBP related structures are also available including structures of MIP (Macrophage Infectivity Potentiator protein) from Legionella pneumophila and Trypanosoma cruzi and Trigger Factor from Mycoplasma genitalium. For all structures discussed in the review a summary of the available biological data is also presented.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcineurin / chemistry
  • Calcium Channels / chemistry
  • Cyclophilin A / chemistry
  • Humans
  • Immunophilins / chemistry*
  • Immunophilins / physiology*
  • Ligands
  • Molecular Sequence Data
  • Protein Binding / physiology*
  • Protein Conformation
  • Protein Folding
  • Sequence Homology, Amino Acid
  • Sirolimus / chemistry

Substances

  • Calcium Channels
  • Ligands
  • Calcineurin
  • Cyclophilin A
  • Immunophilins
  • Sirolimus