1c5f

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[[Image:1c5f.png|left|200px]]
 
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{{STRUCTURE_1c5f| PDB=1c5f | SCENE= }}
{{STRUCTURE_1c5f| PDB=1c5f | SCENE= }}
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===CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A===
===CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A===
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{{ABSTRACT_PUBMED_10642184}}
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==Function==
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[[http://www.uniprot.org/uniprot/CYP1_BRUMA CYP1_BRUMA]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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{{ABSTRACT_PUBMED_10642184}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:010642184</ref><references group="xtra"/>
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<ref group="xtra">PMID:010642184</ref><references group="xtra"/><references/>
[[Category: Brugia malayi]]
[[Category: Brugia malayi]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]

Revision as of 06:40, 10 April 2014

Template:STRUCTURE 1c5f

Contents

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

Template:ABSTRACT PUBMED 10642184

Function

[CYP1_BRUMA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

About this Structure

1c5f is a 16 chain structure with sequence from Brugia malayi. This structure supersedes the now removed PDB entry 1qtl. Full crystallographic information is available from OCA.

Reference

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

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