1FKS

SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN

Summary for 1FKS

• Entry DOI: 10.2210/pdb1fks/pdb
• Descriptor: FK506 AND RAPAMYCIN-BINDING PROTEIN (1 entity in total)
• Functional Keywords: cis-trans isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol : P62942
• Total number of polymer chains: 1
• Total formula weight: 11836.51

Authors

Michnick, S.W.,Rosen, M.K.,Wandless, T.J.,Karplus, M.,Schreiber, S.L. (deposition date: 1992-03-05, release date: 1994-01-31, Last modification date: 2024-05-01)

Primary citation

Michnick, S.W.,Rosen, M.K.,Wandless, T.J.,Karplus, M.,Schreiber, S.L.
Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin.
Science, 252:836-839, 1991

PubMed Abstract: Immunophilins, when complexed to immunosuppressive ligands, appear to inhibit signal transduction pathways that result in exocytosis and transcription. The solution structure of one of these, the human FK506 and rapamycin binding protein (FKBP), has been determined by nuclear magnetic resonance (NMR). FKBP has a previously unobserved antiparallel beta-sheet folding topology that results in a novel loop crossing and produces a large cavity lined by a conserved array of aromatic residues; this cavity serves as the rotamase active site and drug-binding pocket. There are other significant structural features (such as a protruding positively charged loop and an apparently flexible loop) that may be involved in the biological activity of FKBP.

PubMed: 1709301

Experimental method

SOLUTION NMR