Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA

Ryoko Maesaki; Toshiyuki Shimizu; Kentaro Ihara; Shinya Kuroda; Kozo Kaibuchi; Toshio Hakoshima

doi:10.1006/jsbi.1999.4114

Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA

Ryoko Maesaki
, Toshiyuki Shimizu
, Kentaro Ihara
, Shinya Kuroda
, Kozo Kaibuchi
, Toshio Hakoshima

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

7 Citations (Scopus)

Abstract

The effector domain of human protein serine/threonine kinase N (PKN), an effector protein for the small GTP-binding protein Rho, was expressed and purified for protein characterization and crystallization, in a complex form with human RhoA. In solution, RhoA binds to the PKN effector domain with 1:2 stoichiometry in a GTP-dependent manner. The obtained complex crystals diffract to 2.2 Å resolution.

Original language	English
Pages (from-to)	166-170
Number of pages	5
Journal	Journal of Structural Biology
Volume	126
Issue number	2
DOIs	https://doi.org/10.1006/jsbi.1999.4114
Publication status	Published - 15-06-1999
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology

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10.1006/jsbi.1999.4114

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title = "Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA",

abstract = "The effector domain of human protein serine/threonine kinase N (PKN), an effector protein for the small GTP-binding protein Rho, was expressed and purified for protein characterization and crystallization, in a complex form with human RhoA. In solution, RhoA binds to the PKN effector domain with 1:2 stoichiometry in a GTP-dependent manner. The obtained complex crystals diffract to 2.2 {\AA} resolution.",

author = "Ryoko Maesaki and Toshiyuki Shimizu and Kentaro Ihara and Shinya Kuroda and Kozo Kaibuchi and Toshio Hakoshima",

note = "Funding Information: We thank J. Tsukamoto for her technical support in performing MALDI-TOF MS and N-terminal analysis. This work was supported by Grants in Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan to T.H. (10179104, 10359003, 09308025). K.I. was supported by a research fellowship for Young Scientists from JSPS.",

year = "1999",

month = jun,

day = "15",

doi = "10.1006/jsbi.1999.4114",

language = "English",

volume = "126",

pages = "166--170",

journal = "Journal of Structural Biology",

issn = "1047-8477",

publisher = "Academic Press Inc.",

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TY - JOUR

T1 - Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA

AU - Maesaki, Ryoko

AU - Shimizu, Toshiyuki

AU - Ihara, Kentaro

AU - Kuroda, Shinya

AU - Kaibuchi, Kozo

AU - Hakoshima, Toshio

N1 - Funding Information: We thank J. Tsukamoto for her technical support in performing MALDI-TOF MS and N-terminal analysis. This work was supported by Grants in Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan to T.H. (10179104, 10359003, 09308025). K.I. was supported by a research fellowship for Young Scientists from JSPS.

PY - 1999/6/15

Y1 - 1999/6/15

N2 - The effector domain of human protein serine/threonine kinase N (PKN), an effector protein for the small GTP-binding protein Rho, was expressed and purified for protein characterization and crystallization, in a complex form with human RhoA. In solution, RhoA binds to the PKN effector domain with 1:2 stoichiometry in a GTP-dependent manner. The obtained complex crystals diffract to 2.2 Å resolution.

AB - The effector domain of human protein serine/threonine kinase N (PKN), an effector protein for the small GTP-binding protein Rho, was expressed and purified for protein characterization and crystallization, in a complex form with human RhoA. In solution, RhoA binds to the PKN effector domain with 1:2 stoichiometry in a GTP-dependent manner. The obtained complex crystals diffract to 2.2 Å resolution.

UR - https://www.scopus.com/pages/publications/0033563754

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DO - 10.1006/jsbi.1999.4114

M3 - Article

C2 - 10388627

AN - SCOPUS:0033563754

SN - 1047-8477

VL - 126

SP - 166

EP - 170

JO - Journal of Structural Biology

JF - Journal of Structural Biology

IS - 2

ER -

Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA

Abstract

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