Tumor Necrosis Factor-Beta with its Receptor

But first, some info on the structure of TNF-beta!

The overall structure of tumor necrosis factor-beta, also known as human lymphotoxin, is very similar to TNF-alpha. The TNF-beta monomer, which is shown to the right (in blue) with one of its possible receptors (in green), is an all beta-sheet protein as is the TNF-alpha monomer. Push the button to investigate! As you can see, the 171 amino acid TNF-beta monomer has no disulfide bonds, unlike the the TNF-alpha monomer which has 1 (Eck, 1989). In fact, there is only 32% of identical primary sequence between the two TNFs (Eck et al., 1993). This may account for the lack of disulfide bonds in TNF-beta. Another difference between the two is that TNF-beta is a glycoprotein.

The active form of TNF-beta, like its counterpart, is the trimer form (Eck et al., 1993). For another look at the trimer, click here. In fact, in the TNFs, the monomers are arranged together internally to form the trimer in exactly the same way. The surfaces of these two trimers differ everywhere in detail, however. Only 17 surface residues per monomer are conserved (Eck et al., 1993). Both molecules are cytotoxic to some tumor cell lines in vitro and cause hemorrhagic necrosis of tumors in vivo (Gray, et al., 1984).

Click here for more information!
Click here to return to the title page!


Heather Sarauer
Department of Chemistry
University of Wisconsin--Eau Claire


sarauehl@uwec.edu


[UWEC Web] [Schools & Dept.] [Chemistry Dept.]