1c5f

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(New page: 200px<br /><applet load="1c5f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c5f, resolution 2.47&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 10:03, 20 November 2007

Image:1c5f.gif

1c5f, resolution 2.47Å

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CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A

Overview

The resistance of the human parasite Brugia malayi to the antiparasitic, activity of cyclosporin A (CsA) may arise from the presence of, cyclophilins with relatively low affinity for the drug. The structure of, the complex of B. malayi cyclophilin (BmCYP-1) and CsA, with eight, independent copies in the asymmetric unit, has been determined at a, resolution of 2.7 A. The low affinity of BmCYP-1 for CsA arises from, incomplete preorganization of the binding site so that the formation of a, hydrogen bond between His132 of BmCYP-1 and N-methylleucine 9 of CsA is, associated with a shift in the backbone of approximately 1 A in this, region.

About this Structure

1C5F is a Single protein structure of sequence from Brugia malayi. This structure superseeds the now removed PDB entry 1QTL. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin A., Ellis PJ, Carlow CK, Ma D, Kuhn P, Biochemistry. 2000 Jan 25;39(3):592-8. PMID:10642184

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