Fig. 1: Crystal structure of human twisted gastrulation (TWSG1).
From: Molecular mechanism of BMP signal control by Twisted gastrulation
A Domain organization of human TWSG1. Predicted glycosylated asparagine residues (52, 81, and 147) are marked with gray hexagons. B SEC-MALS analysis of TWSG1. The experimentally determined molecular mass of TWSG1 varies from 26,332 to 61,937 Da. Theoretical molecular mass of the TWSG1 monomer is 23,541 Da protein plus 5648 Da Asn-linked glycans (three Man9GlcNAc2 moieties, 1.88264 kDa each). Traces of absorbance at 280 nm and calculated molecular mass are colored in black and red, respectively. C Crystal structure of the human TWSG1 dimer with one protomer colored as rainbow (N-terminus, blue; C-terminus, red) and one in gray. The two views differ by a 180° rotation around a vertical axis. D, E Architecture of the TWSG1 N- and C-terminal domains (NTD and CTD). Disulfide bonds are numbered in Roman numerals and shown as yellow spheres and sticks. F–I SPR-based equilibrium binding experiments. Different concentrations of TWSG1 NTD (black circles), CTD (pink squares), and BSA (aquamarine triangles) were injected over surfaces coated with BMP7 (F), GDF5 (G), BMP2 (H), or CHRDL2 (I). Equilibrium binding dissociation constants (Kds) are indicated. RU response units.
