1W8M
Enzymatic and Structural Characterisation of Non Peptide Ligand Cyclophilin Complexes
Summary for 1W8M
| Entry DOI | 10.2210/pdb1w8m/pdb |
| Related | 1W7Y 1W8L 1W8V |
| Descriptor | PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, ETHYL OXO(PIPERIDIN-1-YL)ACETATE (3 entities in total) |
| Functional Keywords | complex (isomerase-immunosuppressant), non peptide ligand, isomerase, multigene family, rotamase |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm: P62937 |
| Total number of polymer chains | 1 |
| Total formula weight | 18221.72 |
| Authors | Kontopidis, G.,Taylor, P.,Walkinshaw, M. (deposition date: 2004-09-24, release date: 2004-09-30, Last modification date: 2023-12-13) |
| Primary citation | Kontopidis, G.,Taylor, P.,Walkinshaw, M. Enzymatic and Structural Characterization of Non-Peptide Ligand-Cyclophilin Complexes Acta Crystallogr.,Sect.D, 60:479-, 2004 Cited by PubMed Abstract: Piperidine ligands are described that provide the first examples of non-peptidic ligand structures for the cyclophilin family of proteins. Crystal structures of two ligand complexes are compared with the unliganded protein and show ligand-induced changes in side-chain conformation and water binding. A peptidylprolyl cis-trans-isomerase assay showed the dissociation constants of the two ligands to be 320 and 25 mM. This study also provides the first published data for both enzymatic activity and three-dimensional structure for any protein-ligand complex that binds with a high-millimolar dissociation constant. The structures may be of relevance in the field of drug design, as they suggest starting points for the design of larger tighter-binding analogues. PubMed: 14993672DOI: 10.1107/S0907444904000174 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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