2RSE
NMR structure of FKBP12-mTOR FRB domain-rapamycin complex structure determined based on PCS
Summary for 2RSE
| Entry DOI | 10.2210/pdb2rse/pdb |
| NMR Information | BMRB: 11471 |
| Descriptor | Peptidyl-prolyl cis-trans isomerase FKBP1A, Serine/threonine-protein kinase mTOR, TERBIUM(III) ION (3 entities in total) |
| Functional Keywords | fkbp12, rapamycin, fk506, lanthanide, pcs, isomerase-transferase complex, isomerase/transferase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm: P62942 Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side: P42345 |
| Total number of polymer chains | 2 |
| Total formula weight | 23486.29 |
| Authors | Kobashigawa, Y.,Ushio, M.,Saio, T.,Inagaki, F. (deposition date: 2012-01-25, release date: 2012-05-30, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 22487935DOI: 10.1007/s10858-012-9623-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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