Abstract
The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of She complexed to a phosphopeptide reveals an alternative means of recognizing tryosine-phosphorylated proteins. Unlike in SH2 domains, the phosphopeptide forms an antiparallel β-strand with a β-sheet of the protein, interacts with a hydrophobic pocket through the (pY–5) residue, and adopts a β-turn. The PTB domain is structurally similar to pleckstrin homology domains (a β-sandwich capped by an α-helix) and binds to acidic phospholipids, suggesting a possible role in membrane localization.
Originalsprache | Englisch |
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Seiten (von - bis) | 584-592 |
Seitenumfang | 9 |
Fachzeitschrift | Nature |
Jahrgang | 378 |
Ausgabenummer | 6557 |
DOIs | |
Publikationsstatus | Veröffentlicht - 7 Dez. 1995 |
Extern publiziert | Ja |