1cwh

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HUMAN CYCLOPHILIN A COMPLEXED WITH 3-D-SER CYCLOSPORIN

Structural highlights

1cwh is a 2 chain structure with sequence from Homo sapiens and Tolypocladium inflatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.86Å
Ligands:ABA, BMT, DAL, DSE, MLE, MVA
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PPIA_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Eight new X-ray structures of different cyclophilin A/cyclosporin-derivative complexes are presented. These structures, combined with the existing three published cyclosporin complexes, provide a useful structural database for the analysis of protein-ligand interactions. The effect of small chemical differences on protein-ligand hydrogen-bonding, van der Waals interactions and water structure is presented.

X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A.,Kallen J, Mikol V, Taylor P, Walkinshaw MD J Mol Biol. 1998 Oct 23;283(2):435-49. PMID:9769216[1]

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

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See Also

References

  1. ↑ Kallen J, Mikol V, Taylor P, Walkinshaw MD. X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A. J Mol Biol. 1998 Oct 23;283(2):435-49. PMID:9769216

Contents


PDB ID 1cwh

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OCA

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