Figure 1.
FIG. 1. Structures of the Dab DH domain. Overview of
ligand-free Dab2-DH (A), the binary complex of Dab2-DH with the
APP peptide (-7NGYENPTYK+1) (B), and the ternary complex of
Dab1-DH with the same APP peptide and Ins-1,4,5-P[3] (C).
Helices are shown in cyan, strands are shown in yellow, and
other structural elements are shown in brown. The APP peptide is
shown in green, whereas carbons of Ins-1,4,5-P[3] binding
residues are in yellow (ball and stick representations). Note
that the NPXY motif binding site is 25 Å from the
binding site for Ins-1,4,5-P[3], consistent with the possible
simultaneous binding of the Dab DH domain to peptides and to
phosphoinositides (18, 27). D, structural comparison of Dab2-DH
with the other NPXY binding PTB/PI domains Shc and X-11 (left to
right). The top panels show the NPXY peptides (green), Tyr-0
(carbons, green; ball and stick representation), and the
interacting protein residues (carbons, gray; ball and stick
representation). The bottom panels show close-up views of the
Tyr-0-binding site. Hydrogen bonds are indicated by broken lines.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
36572-36581)
copyright 2003.
25 Å from the
binding site for Ins-1,4,5-P[3], consistent with the possible
simultaneous binding of the Dab DH domain to peptides and to
phosphoinositides (18, 27). D, structural comparison of Dab2-DH
with the other NPXY binding PTB/PI domains Shc and X-11 (left to
right). The top panels show the NPXY peptides (green), Tyr-0
(carbons, green; ball and stick representation), and the
interacting protein residues (carbons, gray; ball and stick
representation). The bottom panels show close-up views of the
Tyr-0-binding site. Hydrogen bonds are indicated by broken lines.