Structure and ligand recognition of the phosphotyrosine binding domain of Shc
Authors
Zhou
MM
,
Ravichandran
KS
,
Olejniczak
EF
,
Petros
AM
,
Meadows
RP
,
Sattler
M
,
Harlan
JE
,
Wade
WS
,
Burakoff
SJ
,
Fesik
SW
.
Nature. 1995 12 7; 378(6557).
584-592
Nature. 1995 12 7; 378(6557).
584-592
Abstract
The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of Shc complexed to a phosphopeptide reveals an alternative means of recognizing tyrosine-phosphorylated proteins. Unlike in SH2 domains, the phosphopeptide forms an antiparallel beta-strand with a beta-sheet of the protein, interacts with a hydrophobic pocket through the (pY-5) residue, and adopts a beta-turn. The PTB domain is structurally similar to pleckstrin homology domains (a beta-sandwich capped by an alpha-helix) and binds to acidic phospholipids, suggesting a possible role in membrane localization.