Alkylation of Histidine Residues of Bothrops jararacussu Venom Proteins and Isolated Phospholipases : A Biotechnological Tool to Improve the Production of Antibodies
Figure 6
Preliminary crystal structure of BthTX-I chemically modified by p-bromophenacyl bromide (BPB). (a) Ribbon representation of BthTX-I/BPB structure with the secondary structure elements marked: the Ca2+-binding loop (25 to 34), β-wing (75 to 84), and the three α-helices—“h1” (1 to 12), “h2” (40 to 58), and “h3” (89 to 110). The p-bromophenacyl bromide molecules are highlighted as green sticks. (b) Top view of BPB covalently bound to the His48 residue of the “active site” region of monomers A and B of the BthTX-I/BPB complex. Interactions of BPB with the protein residues are indicated. The sequences have been numbered following Renetseder and coauthors [47]. Molecules were drawn using the PyMOL program [48].
