Abstract
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.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 7:47 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 1:19 p.m.) |
Indexed | 3 weeks, 3 days ago (Aug. 5, 2025, 9:08 a.m.) |
Issued | 33 years, 9 months ago (Nov. 1, 1991) |
Published | 33 years, 9 months ago (Nov. 1, 1991) |
Published Online | 33 years, 9 months ago (Nov. 1, 1991) |
Published Print | 33 years, 9 months ago (Nov. 1, 1991) |
@article{Ke_1991, title={Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution.}, volume={88}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.88.21.9483}, DOI={10.1073/pnas.88.21.9483}, number={21}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Ke, H M and Zydowsky, L D and Liu, J and Walsh, C T}, year={1991}, month=nov, pages={9483–9487} }