Structure determination of a protein assembly by amino acid selective cross-saturation

Eiji Kanamori; Shunsuke Igarashi; Masanori Osawa; Yoshifumi Fukunishi; Ichio Shimada; Haruki Nakamura

doi:10.1002/prot.22871

Structure determination of a protein assembly by amino acid selective cross-saturation

Eiji Kanamori, Shunsuke Igarashi, Masanori Osawa, Yoshifumi Fukunishi, Ichio Shimada, Haruki Nakamura

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

Amino acid selective cross-saturation (ASCS) method not only provides information about the interface of a protein assembly by the spin relaxation experiment, but also identifies the amino acid residues in the acceptor protein, which are located close to the selectively labeled amino acid residues in the donor protein. Here, a new method was developed to build a precise structural model of a protein assembly, which satisfies the experimental ASCS values, using simulated annealing computation. This method was applied to the ubiquitin-yeast ubiquitin hydrolase 1 (Ub-YUH1) complex to build a precise complex structure compatible with that determined by X-ray crystallography. Proteins 2010.

Original language	English
Pages (from-to)	179-190
Number of pages	12
Journal	Proteins: Structure, Function and Bioinformatics
Volume	79
Issue number	1
DOIs	https://doi.org/10.1002/prot.22871
Publication status	Published - 2011 Jan
Externally published	Yes

Keywords

Cross-saturation
Flexible docking
Molecular dynamics
Nuclear magnetic resonance
Protein-protein interaction
Ubiquitin

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.22871

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AU - Kanamori, Eiji

AU - Igarashi, Shunsuke

AU - Osawa, Masanori

AU - Fukunishi, Yoshifumi

AU - Shimada, Ichio

AU - Nakamura, Haruki

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KW - Nuclear magnetic resonance

KW - Protein-protein interaction

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Structure determination of a protein assembly by amino acid selective cross-saturation

Abstract

Keywords

ASJC Scopus subject areas

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