Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein.
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.
Rosen
M K
MK
Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138.
Michnick
S W
SW
Karplus
M
M
Schreiber
S L
SL
D000900:Anti-Bacterial Agents / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D003524:Cyclosporins / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D009584:Nitrogen / Q000737:chemistry*; D011090:Polyenes / Q000737:chemistry*; D011487:Protein Conformation; D011522:Protons; D020123:Sirolimus; D016559:Tacrolimus; D022021:Tacrolimus Binding Proteins
D000900:Anti-Bacterial Agents; D002352:Carrier Proteins; D003524:Cyclosporins; D011090:Polyenes; D011522:Protons; D022021:Tacrolimus Binding Proteins; D009584:Nitrogen; D020123:Sirolimus; D016559:Tacrolimus