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

Kobashigawa, Yoshihiro; Saio, Tomohide; Ushio, Masahiro; Sekiguchi, Mitsuhiro; Yokochi, Masashi; Ogura, Kenji; Inagaki, Fuyuhiko

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

Kobashigawa, Yoshihiro; Saio, Tomohide; Ushio, Masahiro et al.

Journal of Biomolecular NMR, 2012, 53(1), 53-63

Permalink : https://hdl.handle.net/2115/49373

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アクセス権	open access
URI	https://hdl.handle.net/2115/49373
タイトル	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
著者	Kobashigawa, Yoshihiro ; Saio, Tomohide ; Ushio, Masahiro ; Sekiguchi, Mitsuhiro ; Yokochi, Masashi ; Ogura, Kenji ; Inagaki, Fuyuhiko
著者名 Kobashigawa, Yoshihiro
著者名 Saio, Tomohide
著者名 Ushio, Masahiro
著者名 Sekiguchi, Mitsuhiro
著者名 Yokochi, Masashi
e-Rad_Researcher 50270682 著者名 Ogura, Kenji
e-Rad_Researcher 70011757 著者名 Inagaki, Fuyuhiko
言語	英語
キーワード	Differential scanning fluorometry
	Pseudo contact shift
	Lanthanide binding tag
	FKBP12
	FRB
	mTOR
発行日	2012-05
出版者	Springer Netherlands
収録物名	Journal of Biomolecular NMR
巻(号)	53(1)
ページ	53-63
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
PISSN	0925-2738
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.1007/s10858-012-9623-8