1FKR

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

1FKR の概要

• エントリーDOI: 10.2210/pdb1fkr/pdb
• 分子名称: FK506 AND RAPAMYCIN-BINDING PROTEIN (1 entity in total)
• 機能のキーワード: cis-trans isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytosol : P62942
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11836.51

構造登録者

Michnick, S.W.,Rosen, M.K.,Wandless, T.J.,Karplus, M.,Schreiber, S.L. (登録日: 1992-03-05, 公開日: 1994-01-31, 最終更新日: 2024-05-01)

主引用文献

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

実験手法

SOLUTION NMR