1c5f: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1c5f.gif|left|200px]]<br /><applet load="1c5f" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1c5f, resolution 2.47&Aring;" />
caption="1c5f, resolution 2.47&Aring;" />
'''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, 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.
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 superseeds 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C5F OCA].  
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.K.S.]]
[[Category: Carlow, C K.S.]]
[[Category: Ellis, P.J.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:10:23 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:33 2008''