Solution structure of an atypical WW domain in a novel β-clam-like dimeric form

Satoshi Ohnishi; Peter Güntert; Seizo Koshiba; Tadashi Tomizawa; Ryogo Akasaka; Naoya Tochio; Manami Sato; Makoto Inoue; Takushi Harada; Satoru Watanabe; Akiko Tanaka; Mikako Shirouzu; Takanori Kigawa; Shigeyuki Yokoyama

doi:10.1016/j.febslet.2007.01.008

Solution structure of an atypical WW domain in a novel β-clam-like dimeric form

Satoshi Ohnishi, Peter Güntert, Seizo Koshiba, Tadashi Tomizawa, Ryogo Akasaka, Naoya Tochio, Manami Sato, Makoto Inoue, Takushi Harada, Satoru Watanabe, Akiko Tanaka, Mikako Shirouzu, Takanori Kigawa, Shigeyuki Yokoyama

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

32 Citations (Scopus)

Abstract

The WW domain is known as one of the smallest protein modules with a triple-stranded β-sheet fold. Here, we present the solution structure of the second WW domain from the mouse salvador homolog 1 protein. This WW domain forms a homodimer with a β-clam-like motif, as evidenced by size exclusion chromatography, analytical ultracentrifugation and NMR spectroscopy. While typical WW domains are believed to function as monomeric modules that recognize proline-rich sequences, by using conserved aromatic and hydrophobic residues that are solvent-exposed on the surface of the β-sheet, this WW domain buries these residues in the dimer interface.

Original language	English
Pages (from-to)	462-468
Number of pages	7
Journal	FEBS Letters
Volume	581
Issue number	3
DOIs	https://doi.org/10.1016/j.febslet.2007.01.008
Publication status	Published - 2007 Feb 6
Externally published	Yes

Keywords

Homodimer
NMR
Salvador homolog 1 protein
WW domain

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2007.01.008

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title = "Solution structure of an atypical WW domain in a novel β-clam-like dimeric form",

abstract = "The WW domain is known as one of the smallest protein modules with a triple-stranded β-sheet fold. Here, we present the solution structure of the second WW domain from the mouse salvador homolog 1 protein. This WW domain forms a homodimer with a β-clam-like motif, as evidenced by size exclusion chromatography, analytical ultracentrifugation and NMR spectroscopy. While typical WW domains are believed to function as monomeric modules that recognize proline-rich sequences, by using conserved aromatic and hydrophobic residues that are solvent-exposed on the surface of the β-sheet, this WW domain buries these residues in the dimer interface.",

keywords = "Homodimer, NMR, Salvador homolog 1 protein, WW domain",

author = "Satoshi Ohnishi and Peter G{\"u}ntert and Seizo Koshiba and Tadashi Tomizawa and Ryogo Akasaka and Naoya Tochio and Manami Sato and Makoto Inoue and Takushi Harada and Satoru Watanabe and Akiko Tanaka and Mikako Shirouzu and Takanori Kigawa and Shigeyuki Yokoyama",

note = "Funding Information: We thank M. Sato, Y. Ide, M. Kato, A. Hiyoshi and S. Morita for sample preparation. This work was supported by the RIKEN Structural Genomics/Proteomics Initiative (RSGI) and by the National Project on Protein Structural and Functional Analyses, Ministry of Education, Culture, Sports, Science and Technology of Japan.",

year = "2007",

month = feb,

day = "6",

doi = "10.1016/j.febslet.2007.01.008",

language = "English",

volume = "581",

pages = "462--468",

journal = "FEBS Letters",

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TY - JOUR

T1 - Solution structure of an atypical WW domain in a novel β-clam-like dimeric form

AU - Ohnishi, Satoshi

AU - Güntert, Peter

AU - Koshiba, Seizo

AU - Tomizawa, Tadashi

AU - Akasaka, Ryogo

AU - Tochio, Naoya

AU - Sato, Manami

AU - Inoue, Makoto

AU - Harada, Takushi

AU - Watanabe, Satoru

AU - Tanaka, Akiko

AU - Shirouzu, Mikako

AU - Kigawa, Takanori

AU - Yokoyama, Shigeyuki

N1 - Funding Information: We thank M. Sato, Y. Ide, M. Kato, A. Hiyoshi and S. Morita for sample preparation. This work was supported by the RIKEN Structural Genomics/Proteomics Initiative (RSGI) and by the National Project on Protein Structural and Functional Analyses, Ministry of Education, Culture, Sports, Science and Technology of Japan.

PY - 2007/2/6

Y1 - 2007/2/6

N2 - The WW domain is known as one of the smallest protein modules with a triple-stranded β-sheet fold. Here, we present the solution structure of the second WW domain from the mouse salvador homolog 1 protein. This WW domain forms a homodimer with a β-clam-like motif, as evidenced by size exclusion chromatography, analytical ultracentrifugation and NMR spectroscopy. While typical WW domains are believed to function as monomeric modules that recognize proline-rich sequences, by using conserved aromatic and hydrophobic residues that are solvent-exposed on the surface of the β-sheet, this WW domain buries these residues in the dimer interface.

AB - The WW domain is known as one of the smallest protein modules with a triple-stranded β-sheet fold. Here, we present the solution structure of the second WW domain from the mouse salvador homolog 1 protein. This WW domain forms a homodimer with a β-clam-like motif, as evidenced by size exclusion chromatography, analytical ultracentrifugation and NMR spectroscopy. While typical WW domains are believed to function as monomeric modules that recognize proline-rich sequences, by using conserved aromatic and hydrophobic residues that are solvent-exposed on the surface of the β-sheet, this WW domain buries these residues in the dimer interface.

KW - Homodimer

KW - NMR

KW - Salvador homolog 1 protein

KW - WW domain

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U2 - 10.1016/j.febslet.2007.01.008

DO - 10.1016/j.febslet.2007.01.008

M3 - Article

C2 - 17239860

AN - SCOPUS:33846426840

SN - 0014-5793

VL - 581

SP - 462

EP - 468

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Solution structure of an atypical WW domain in a novel β-clam-like dimeric form

Abstract

Keywords

ASJC Scopus subject areas

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