Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein.

Article Details

Citation

Rosen MK, Michnick SW, Karplus M, Schreiber SL

Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein.

Biochemistry. 1991 May 14;30(19):4774-89.

PubMed ID
1709363 [ View in PubMed
]
Abstract

Sequential 1H and 15N assignments of human FKBP, a cytosolic binding protein for the immunosuppressive agents FK506 and rapamycin, are reported. A combination of homonuclear and relayed heteronuclear experiments has enabled assignment of 98 of 99 backbone amide NHs, 119 of 120 C alpha Hs, 97 of 99 non-proline amide 15Ns, and 375 of 412 side-chain resonances of this 107-residue protein. Long-range NOEs are used to demonstrate that FKBP has a novel folding topology consisting of a five-stranded antiparallel beta sheet with +3, +1, -3, +1 loop connectivity.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Peptidyl-prolyl cis-trans isomerase FKBP1AP62942Details