1IIP
Bovine Cyclophilin 40, Tetragonal Form
Summary for 1IIP
Entry DOI | 10.2210/pdb1iip/pdb |
Related | 1IHG |
Descriptor | Cyclophilin 40, GLYCEROL (3 entities in total) |
Functional Keywords | ppiase immunophilin tetratricopeptide, isomerase |
Biological source | Bos taurus (cattle) |
Cellular location | Cytoplasm: P26882 |
Total number of polymer chains | 1 |
Total formula weight | 40770.41 |
Authors | Taylor, P.,Dornan, J.,Carrello, A.,Minchin, R.F.,Ratajczak, T.,Walkinshaw, M.D. (deposition date: 2001-04-24, release date: 2001-05-16, Last modification date: 2024-11-06) |
Primary citation | Taylor, P.,Dornan, J.,Carrello, A.,Minchin, R.F.,Ratajczak, T.,Walkinshaw, M.D. Two structures of cyclophilin 40: folding and fidelity in the TPR domains. Structure, 9:431-438, 2001 Cited by PubMed Abstract: The "large immunophilin" family consists of domains of cyclophilin or FK506 binding protein linked to a tetratricopeptide (TPR) domain. They are intimately associated with steroid receptor complexes and bind to the C-terminal domain of Hsp90 via the TPR domain. The competitive binding of specific large immunophilins and other TPR-Hsp90 proteins provides a regulatory mechanism for Hsp90 chaperone activity. PubMed: 11377203DOI: 10.1016/S0969-2126(01)00603-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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