(Downloading may take up to 30 seconds.
If the slide opens in your browser, select File -> Save As to save it.)
Click on image to view larger version.



Fig. 1. The TGFß large latent complex (LLC). The LLC comprises TGFß (black), LAP (red) and LTBP. TGFß and LAP are proteolytically separated at the site indicated by the arrowhead. After processing, TGFß remains noncovalently associated with LAP. LAP and LTBP are joined by disulfide bonds (light blue lines). The LLC is covalently linked to the extracellular matrix (ECM) through an isopeptide bond (green) between the N-terminus of LTBP (somewhere between EGF2 and the hinge domain) and a currently unidentified matrix protein. The hinge domain (arrow) of LTBP is a protease-sensitive region that allows LLC to be proteolytically released from the ECM.