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    Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9483-7.

    Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution.

    Ke HM, Zydowsky LD, Liu J, Walsh CT.

    Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill 27599.

    The structure of the unligated human T-cell recombinant cyclophilin has been determined at 3 A resolution by multipole isomorphous replacement methods and refined at 2.5 A resolution to an R factor of 0.209. The root-mean-square errors of the bond lengths and bond angles are 0.013 A and 2.8 degrees from ideal geometry, respectively. The overall structure is a beta-barrel, consisting of eight antiparallel beta-strands wrapping around the barrel surface and two alpha-helices sitting on the top and the bottom closing the barrel. Inside the barrel, seven aromatic and other hydrophobic residues form a compact hydrophobic core. A loop of Lys-118 to His-126 and four beta-strands (B3-B6) constitute a pocket we speculate to be the binding site of cyclosporin A.

    PMID: 1946361 [PubMed - indexed for MEDLINE]

    PMCID: 52742

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