Fig. 3
From: MANF antagonizes nucleotide exchange by the endoplasmic reticulum chaperone BiP
Crystal structure of BiP NBD in complex with MANF or SAP. a Superimposed structures of BiP NBD in complex with MANF or the isolated SAP domain (silver) showing the same binding interface between SAP and NBD (RMSD = 1.3 Å over 379 Cα atoms). The NBD–SAP complex is colored in gray, while MANF is gold and its bound NBD is blue. b Overlay of the NBD–MANF complex (from a) with full-length BiP (in the ATP state, yellow; PDB 5E84) aligned by their NBD. Note the steric clashes between SAP and the BiP interdomain linker (colored red). c Overlay of the NBD–MANF complex (from a) and one state of the solution structure of DnaK in the apo/ADP conformation (green; PDB 2KHO) aligned by their NBD. Note that in the domain-undocked (apo/ADP) state, Hsp70 (DnaK) accommodates the binding of MANF to its NBD. d Overlay of the NBD–MANF complex (from a) onto the structure of apo BiPV461F. MANF (gold) can be accommodated by an individual BiP molecule (magenta) in the extended, domain-undocked conformation, while a significant steric clash is noted with a crystallographic symmetry-related BiP molecule (cyan), which contacts the interdomain linker of the former BiP (magenta)
