Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution.
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.
Ke
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Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill 27599.
Zydowsky
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LD
Liu
J
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Walsh
C T
CT
D000591:Amino Acid Isomerases / Q000737:chemistry*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry*; D003196:Computer Graphics; D003461:Crystallography; D016572:Cyclosporine / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D019696:Peptidylprolyl Isomerase; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D012995:Solubility; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D011994:Recombinant Proteins; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase