Results: 4

1.
Figure 3

Figure 3. From: The VPAC1 receptor: structure and function of a class B GPCR prototype.

The 3D-structural model of VPAC1 receptor N-ted and docking of VIP. Ribbon representation of the VPAC1 N-ted: light gray ribbon, main chain; white ribbon, VIP. Docking calculations showed that Q135, D107, G116, C122, and K127 residues (middle gray sticks) present in the N-ted were in contact (white arrows) with the side chains of F0, F6, Y22, N24, and N28 (black sticks) of VIP residues, respectively. Figure was obtained by using PyMOL software (http://www.pymol.org).

A. Couvineau, et al. Front Endocrinol (Lausanne). 2012;3:139.
2.
Figure 4

Figure 4. From: The VPAC1 receptor: structure and function of a class B GPCR prototype.

Representation of global 3D-model of VPAC1 docked to VIP. (A) 3D-global model of human VPAC1 based on X-ray structure of the A2A receptor. (B) Upside view of 3D-global model of human VPAC1 displaying side-chains of residues of the 3D-global model of the receptor (black sticks) in close contact (distance <6Å) with the N-terminal end of VIP (white). middle gray ribbon, transmembrane domains; black ribbon, main chain of N-ted; white ribbon, main chain of VIP.

A. Couvineau, et al. Front Endocrinol (Lausanne). 2012;3:139.
3.
Figure 2

Figure 2. From: The VPAC1 receptor: structure and function of a class B GPCR prototype.

NMR structure of VIP and representation of N-capping motif. Middle gray ribbon represents the average conformation of VIP structure. In magnified inset the N-capping motif is represented as (1) the hydrophobic interactions between side-chain groups of N' and N3 residues (dashed lines); (2) the hydrogen bond between side chain of N-cap residue and backbone atom of N3 residue. See ref. Neumann et al. (2008) for details.

A. Couvineau, et al. Front Endocrinol (Lausanne). 2012;3:139.
4.
Figure 1

Figure 1. From: The VPAC1 receptor: structure and function of a class B GPCR prototype.

Representation of generic Sushi domain core of Class B GPCR N-ted. Common structural elements of class B GPCR N-ted are represented by the presence of (1) a N-terminal α-helix (black ribbon); (2) two anti-parallel β-sheets (β1-β2 and β3-β4, black ribbon). The Sushi domain structural core is stabilized by the presence of three conserved disulfide bonds (middle gray sticks) and represented in magnified inset an ionic and hydrophobic interactions (light gray sticks). All figures were obtained by using PyMOL software (http://www.pymol.org).

A. Couvineau, et al. Front Endocrinol (Lausanne). 2012;3:139.

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