PDBsum entry 2ela

Cell cycle

PDB id: 2ela

Contents

Protein chains

131 a.a. *

141 a.a. *

Waters ×236

* Residue conservation analysis

PDB id:

2ela

Name:

Cell cycle

Title:

Crystal structure of the ptb domain of human appl1

Structure:

Adapter protein containing ph domain, ptb domain and leucine zipper motif 1. Chain: a, b. Fragment: ptb domain. Synonym: appl1, dip13 alpha, dcc-interacting protein 13 alpha. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.222 R-free: 0.259

Authors:

J.Li,X.Mao,L.Q.Dong,F.Liu,L.Tong

Key ref:

J.Li et al. (2007). Crystal Structures of the BAR-PH and PTB Domains of Human APPL1. Structure, 15, 525-533. PubMed id: 17502098 DOI: 10.1016/j.str.2007.03.011

Date:

27-Mar-07 Release date: 29-May-07

Protein chain

Q9UKG1  (DP13A_HUMAN) -  DCC-interacting protein 13-alpha from Homo sapiens

Seq: 709 a.a.

Struc: 131 a.a.

Protein chain

Q9UKG1  (DP13A_HUMAN) -  DCC-interacting protein 13-alpha from Homo sapiens

Seq: 709 a.a.

Struc: 141 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1016/j.str.2007.03.011

Structure 15:525-533 (2007)

PubMed id: 17502098

Crystal Structures of the BAR-PH and PTB Domains of Human APPL1.

J.Li, X.Mao, L.Q.Dong, F.Liu, L.Tong.

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.

Selected figure(s)

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.

Figures were selected by an automated process.