Jacqueline Dornan, Paul Taylor and Malcolm D. Walkinshaw Pages 1392 - 1409 ( 18 )
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.
comparison of x-ray, nmr structures of cyclophilins and fkbps, variation among species, families of cyclophilin ligands and their structures, families of fkbp ligands and their structures, immunophilin protein complexes
Structural Biochemistry, The University of Edinburgh, Michael Swann Building, King's Buildings,Edinburgh, EH9 3JR, UK.