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1dyw
From Proteopedia
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BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A DIVERGENT LOOP CYCLOPHILIN FROM CAENORHABDITIS ELEGANS
Overview
Cyclophilin 3 (CYP-3) is one of the most abundantly expressed cyclophilin, isoforms in the free living nematode Caenorhabditis elegans. The detailed, post-embryonic expression pattern of the cyp-3 transcript is unusual, peaking during early larval development. The spatial expression pattern, was examined via reporter gene analysis demonstrating that the cyp-3, transcript is exclusively expressed in the single anterior excretory cell., Recombinant cyclophilin 3 has been purified, crystallized and solved to a, resolution of 1.8 A. The peptidyl-prolyl isomerase activity of CYP-3 has, been characterized against the substrate, N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, and gives a k(cat)/K(m) value, of 2.4 x 10(6) M(-1) s(-1). The immunosuppressive drug cyclosporin A binds, and inhibits CYP-3 ... [(full description)]
About this Structure
1DYW is a [Single protein] structure of sequence from [Caenorhabditis elegans]. Active as [Peptidylprolyl isomerase], with EC number [5.2.1.8]. Structure known Active Site: CBS. Full crystallographic information is available from [OCA].
Reference
Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans., Dornan J, Page AP, Taylor P, Wu S, Winter AD, Husi H, Walkinshaw MD, J Biol Chem. 1999 Dec 3;274(49):34877-83. PMID:10574961
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