2RSE

NMR structure of FKBP12-mTOR FRB domain-rapamycin complex structure determined based on PCS

2RSE の概要

• エントリーDOI: 10.2210/pdb2rse/pdb
• NMR情報: BMRB: 11471
• 分子名称: Peptidyl-prolyl cis-trans isomerase FKBP1A, Serine/threonine-protein kinase mTOR, TERBIUM(III) ION (3 entities in total)
• 機能のキーワード: fkbp12, rapamycin, fk506, lanthanide, pcs, isomerase-transferase complex, isomerase/transferase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P62942; Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side: P42345
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23486.29

構造登録者

Kobashigawa, Y.,Ushio, M.,Saio, T.,Inagaki, F. (登録日: 2012-01-25, 公開日: 2012-05-30, 最終更新日: 2024-05-15)

主引用文献

Kobashigawa, Y.,Saio, T.,Ushio, M.,Sekiguchi, M.,Yokochi, M.,Ogura, K.,Inagaki, F.
Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.
J.Biomol.Nmr, 53:53-63, 2012

PubMed Abstract: Pseudo contact shifts (PCSs) induced by paramagnetic lanthanide ions fixed in a protein frame provide long-range distance and angular information, and are valuable for the structure determination of protein-protein and protein-ligand complexes. We have been developing a lanthanide-binding peptide tag (hereafter LBT) anchored at two points via a peptide bond and a disulfide bond to the target proteins. However, the magnetic susceptibility tensor displays symmetry, which can cause multiple degenerated solutions in a structure calculation based solely on PCSs. Here we show a convenient method for resolving this degeneracy by changing the spacer length between the LBT and target protein. We applied this approach to PCS-based rigid body docking between the FKBP12-rapamycin complex and the mTOR FRB domain, and demonstrated that degeneracy could be resolved using the PCS restraints obtained from two-point anchored LBT with two different spacer lengths. The present strategy will markedly increase the usefulness of two-point anchored LBT for protein complex structure determination.

PubMed: 22487935
DOI: 10.1007/s10858-012-9623-8

実験手法

SOLUTION NMR