The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi

Paul Taylor; Antony P. Page; George Kontopidis; Holger Husi; Malcolm D. Walkinshaw

doi:10.1016/S0014-5793(98)00264-6

The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi

Paul Taylor, Antony P. Page, George Kontopidis, Holger Husi, Malcolm D. Walkinshaw

Division of Biomedical Sciences

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Abstract

A structure of residues 1-177 of the cyclophilin domain of a large divergent cyclophilin from the filarial nematode parasite Brugia malayi has been crystallised and solved in two different crystal forms. The active site has a similar structure to that of human cyclophilin A. Two of the 13 residues important in forming the human cyclophilin A/cyclosporin A complex are altered in the B. malayi cyclophilin and explain the relatively poor inhibition of peptidyl prolyl isomerase activity by cyclosporin A.

Original language	English
Pages (from-to)	361-366
Number of pages	6
Journal	FEBS Letters
Volume	425
Issue number	2
DOIs	https://doi.org/10.1016/S0014-5793(98)00264-6
Publication status	Published - 1 Mar 1998

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title = "The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi",

abstract = "A structure of residues 1-177 of the cyclophilin domain of a large divergent cyclophilin from the filarial nematode parasite Brugia malayi has been crystallised and solved in two different crystal forms. The active site has a similar structure to that of human cyclophilin A. Two of the 13 residues important in forming the human cyclophilin A/cyclosporin A complex are altered in the B. malayi cyclophilin and explain the relatively poor inhibition of peptidyl prolyl isomerase activity by cyclosporin A.",

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T1 - The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi

AU - Taylor, Paul

AU - Page, Antony P.

AU - Kontopidis, George

AU - Husi, Holger

AU - Walkinshaw, Malcolm D.

PY - 1998/3/1

Y1 - 1998/3/1

N2 - A structure of residues 1-177 of the cyclophilin domain of a large divergent cyclophilin from the filarial nematode parasite Brugia malayi has been crystallised and solved in two different crystal forms. The active site has a similar structure to that of human cyclophilin A. Two of the 13 residues important in forming the human cyclophilin A/cyclosporin A complex are altered in the B. malayi cyclophilin and explain the relatively poor inhibition of peptidyl prolyl isomerase activity by cyclosporin A.

AB - A structure of residues 1-177 of the cyclophilin domain of a large divergent cyclophilin from the filarial nematode parasite Brugia malayi has been crystallised and solved in two different crystal forms. The active site has a similar structure to that of human cyclophilin A. Two of the 13 residues important in forming the human cyclophilin A/cyclosporin A complex are altered in the B. malayi cyclophilin and explain the relatively poor inhibition of peptidyl prolyl isomerase activity by cyclosporin A.

U2 - 10.1016/S0014-5793(98)00264-6

DO - 10.1016/S0014-5793(98)00264-6

M3 - Article

SN - 1873-3468

VL - 425

SP - 361

EP - 366

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi

Abstract

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