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1W8L

Enzymatic and structural characterization of non peptide ligand cyclophilin complexes

Summary for 1W8L
Entry DOI10.2210/pdb1w8l/pdb
Related1W7Y 1W8M 1W8V
DescriptorPEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, (3R)-1-ACETYL-3-METHYLPIPERIDINE (3 entities in total)
Functional Keywordscomplex (isomerase-immunosuppressant), non-peptide ligand, isomerase, multigene family, rotamase
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains1
Total formula weight18177.72
Authors
Kontopidis, G.,Taylor, P.,Walkinshaw, M. (deposition date: 2004-09-23, release date: 2004-09-30, Last modification date: 2023-12-13)
Primary citationKontopidis, G.,Taylor, P.,Walkinshaw, M.
Enzymatic and Structural Characterization of Non-Peptide Ligand-Cyclophilin Complexes
Acta Crystallogr.,Sect.D, 60:479-485, 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: 14993672
DOI: 10.1107/S0907444904000174
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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