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Structures of immunophilins and their ligand complexes
Jacqueline Dornan1, Paul Taylor, Malcolm D Walkinshaw
1Structural Biochemistry, The University of Edinburgh, Michael Swann Building, King's Buildings, Edinburgh EH9 3JR, Scotland, UK. M.WALKINSHAW@ed.ac.uk
Current Topics in Medicinal Chemistry
|July 23, 2003
Summary
This review analyzes X-ray and NMR structures of immunophilins, including cyclophilins and FK-506 binding proteins (FKBPs). It compares structural features and interactions with small molecule ligands, providing biological context for over 100 protein entries.
Area of Science:
- Structural biology
- Biochemistry
- Immunology
Background:
- Immunophilins, comprising cyclophilins and FK-506 binding proteins (FKBPs), are crucial cellular proteins.
- Their structures are key to understanding their diverse biological functions, including roles in protein folding and immune response.
Purpose of the Study:
- To review and compare available X-ray and NMR structures of cyclophilins and FKBPs.
- To analyze structural features within and between species.
- To present an overview of complexes formed with small molecule ligands, particularly immunosuppressive drugs.
Main Methods:
- Comparative analysis of existing X-ray and NMR crystallographic data.
- Examination of structural data from the Protein Data Base (PDB).
- Integration of structural findings with available biological data.
Main Results:
- Over 60 PDB entries for cyclophilins and over 40 for FKBPs were analyzed.
- Distinct structural features within and across species for both immunophilin families were identified.
- Structures of FKBP-related proteins, including MIP and Trigger Factor, were also considered.
Conclusions:
- Structural diversity exists within cyclophilin and FKBP families.
- Understanding these structures provides insights into their interactions with ligands and biological roles.
- This review consolidates structural and biological information on immunophilins and related proteins.