1c5f
From Proteopedia
(New page: 200px<br /><applet load="1c5f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c5f, resolution 2.47Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1c5f.gif|left|200px]]<br /><applet load="1c5f" size=" | + | [[Image:1c5f.gif|left|200px]]<br /><applet load="1c5f" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c5f, resolution 2.47Å" /> | caption="1c5f, resolution 2.47Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A'''<br /> | '''CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The resistance of the human parasite Brugia malayi to the antiparasitic | + | 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== | ==About this Structure== | ||
| - | 1C5F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brugia_malayi Brugia malayi]. This structure | + | 1C5F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brugia_malayi Brugia malayi]. This structure supersedes the now removed PDB entry 1QTL. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carlow, C | + | [[Category: Carlow, C K.S.]] |
| - | [[Category: Ellis, P | + | [[Category: Ellis, P J.]] |
[[Category: Kuhn, P.]] | [[Category: Kuhn, P.]] | ||
[[Category: Ma, D.]] | [[Category: Ma, D.]] | ||
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[[Category: peptidylprolyl isomerase]] | [[Category: peptidylprolyl isomerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:33 2008'' |
Revision as of 10:02, 21 February 2008
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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 supersedes 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
Page seeded by OCA on Thu Feb 21 12:02:33 2008
