Figure 1

Structure of lipid-bound PASb-3α.
(a) High structural identity between the main chain tracing of PASb-3α and the PASb domains of both HIF-1α and HIF-2α (similar core r.m.s.d. of 0.6 Å). (b) However, a 510 Å3 hydrophobic cavity was exclusively identified in the core of PASb-3α (delimited by gray surface) and (c) found to enclose a monoacylglycerol molecule. (d) Extensive network of polar contacts (yellow dashed lines) shared by specific residues in PASb-3α with the lipid and a neighbor sulfate ion, suggesting that minor rearrangements in the protein may allow for binding of phospholipids.