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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

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Title: 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
Authors: Kobashigawa, Yoshihiro Browse this author
Saio, Tomohide Browse this author
Ushio, Masahiro Browse this author
Sekiguchi, Mitsuhiro Browse this author
Yokochi, Masashi Browse this author
Ogura, Kenji Browse this author →KAKEN DB
Inagaki, Fuyuhiko Browse this author →KAKEN DB
Keywords: Differential scanning fluorometry
Pseudo contact shift
Lanthanide binding tag
FKBP12
FRB
mTOR
Issue Date: May-2012
Publisher: Springer Netherlands
Journal Title: Journal of Biomolecular NMR
Volume: 53
Issue: 1
Start Page: 53
End Page: 63
Publisher DOI: 10.1007/s10858-012-9623-8
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.
Type: article
URI: http://hdl.handle.net/2115/49373
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 稲垣 冬彦

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