 |
PDBsum entry 2elb
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein binding
|
PDB id
|
|
|
|
2elb
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structures of the bar-Ph and ptb domains of human appl1.
|
|
|
Authors
|
|
J.Li,
X.Mao,
L.Q.Dong,
F.Liu,
L.Tong.
|
|
|
Ref.
|
|
Structure, 2007,
15,
525-533.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
APPL1 interacts with adiponectin receptors and other important signaling
molecules. It contains a BAR and a PH domain near its N terminus, and the two
domains may function as a unit (BAR-PH domain). We report here the crystal
structures of the BAR-PH and PTB domains of human APPL1. The structures reveal
novel features for BAR domain dimerization and for the interactions between the
BAR and PH domains. The BAR domain dimer of APPL1 contains two four-helical
bundles, whereas other BAR domain dimers have only three helices in each bundle.
The PH domain is located at the opposite ends of the BAR domain dimer. Yeast
two-hybrid assays confirm the interactions between the BAR and PH domains. Lipid
binding assays show that the BAR, PH, and PTB domains can bind phospholipids.
The ability of APPL1 to interact with multiple signaling molecules and
phospholipids supports an important role for this adaptor in cell signaling.
|
|
|
|
|
|
|
|
Figure 2.
Figure 2. Structure of the BAR-PH Domain Dimer of Human APPL1
(A) Schematic representation of the BAR-PH domain dimer.
One monomer is shown in yellow and the other in cyan.
(B)
The dimer after 90° rotation around the horizontal axis,
showing the banana shape of the structure. The red star
indicates the location of the β1-β2 loop in the PH domain,
which is near the putative phospholipid binding site.
(C)
Superposition of the APPL1 BAR domain dimer (in yellow and cyan)
and that of endophilin (in gray). The red arrow highlights the
structural differences between the two dimers. Produced with
PyMOL (DeLano, 2002).
|
|
Figure 4.
Figure 4. Molecular Surface of the BAR-PH Domain of APPL1
(A) The side view of the molecular surface of the BAR-PH
domain. Strictly conserved basic residues are colored in dark
blue, and basic residues conserved only in APPL1 and APPL2 are
in light blue. The diameter of the BAR-PH dimer is about 170
Å.
(B) The top view of the molecular surface of the
BAR-PH domain. There is a cluster of positively charged residues
near the BAR-PH interface. Produced with PyMOL (DeLano, 2002).
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Structure
(2007,
15,
525-533)
copyright 2007.
|
|
|
|
|
|
|
