Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form.
The WW domain is known as one of the smallest protein modules with a triple-stranded beta-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 beta-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 beta-sheet, this WW domain buries these residues in the dimer interface.
Ohnishi
Satoshi
S
Genomic Sciences Center, RIKEN, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Güntert
Peter
P
Koshiba
Seizo
S
Tomizawa
Tadashi
T
Akasaka
Ryogo
R
Tochio
Naoya
N
Sato
Manami
M
Inoue
Makoto
M
Harada
Takushi
T
Watanabe
Satoru
S
Tanaka
Akiko
A
Shirouzu
Mikako
M
Kigawa
Takanori
T
Yokoyama
Shigeyuki
S
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019281:Dimerization; D066298:In Vitro Techniques; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D013816:Thermodynamics
D018797:Cell Cycle Proteins; D011994:Recombinant Proteins; C485935:Sav1 protein, mouse; D012996:Solutions