Figure 1
From: Use of cyclic peptides to induce crystallization: case study with prolyl hydroxylase domain 2
PHD2 crystallizes as a homotrimer with bicyclic ligands. (A) The homotrimeric crystal packing observed in the nPHD2/P63 crystal structure (PDB ID: 4BQX). (B) The PHD2 homotrimer is stabilised by intermolecular interactions between the active site residues including from the N-terminal β2/β3 loop (aa 237–254) and the C-terminal helix α4 (aa 393–402) of a threefold symmetry related molecule. The overall PHD2 (aa 188–404) fold consists of the major (β1, β8, β5, β10, β4) and minor (β7, β6, β9, β-II) β-sheets of the DSBH, and four α helices. Both the β2/β3 ‘finger’ loop and the C-terminal helix α4 of the PHDs directly interact with the HIF-α ODDs (see Fig. 4).
