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1w8v

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1w8v, resolution 1.70Å ()
Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8
Related: 1w7y, 1w8l, 1w8m
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES

Publication Abstract from PubMed

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.

Enzymatic and structural characterization of non-peptide ligand-cyclophilin complexes., Kontopidis G, Taylor P, Walkinshaw MD, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):479-85. Epub 2004, Feb 25. PMID:14993672

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1w8v is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Kontopidis G, Taylor P, Walkinshaw MD. Enzymatic and structural characterization of non-peptide ligand-cyclophilin complexes. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):479-85. Epub 2004, Feb 25. PMID:14993672 doi:http://dx.doi.org/10.1107/S0907444904000174

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