Figure 1
From: Griffithsin tandemers: flexible and potent lectin inhibitors of the human immunodeficiency virus
Structure and binding site orientation of dimeric GRFT and mutations used to generate monomeric GRFT. Dimeric GRFT (A) is a domain-swapped dimer with two identical carbohydrate-binding domains (circled in blue) separated by 50 Å and at a relative angle of ~160° from each other. Obligate monomeric GRFT (B) was generated by the addition of Gly-Ser residues in the hinge region of wild-type GRFT. The enhanced flexibility of the hinge region resulted in the collapse of the swapped domain to form an obligate monomer, mGRFT.