Enrico Di Cera, M.D., published a review article in the new journal Biophysics Review entitled “Mechanisms of ligand binding.” The review discusses the basic concepts of ligand binding and how these concepts have impacted understanding of binding mechanisms today.
Two main concepts are used to interpret binding data. The first, induced fit, is based on the assumption that the initial binding step induces changes in conformation that enhance the ligand/target comples. The second, conformational selection, assumes that the target exists in multiple conformations and the ligand binds to the target conformation that is most optimal. Taken together, these two concepts can be used to describe and interpret a variety of ligand binding schemes.
Read the full article in Biophysics Review.
(A) Rapid kinetics of FPR binding to prothrombin (closed circles), prethrombin-1 (mixed circles), and prethrombin-2 (open circles).
(B) Crystal structure of prothrombin that reveals the multi-domain architecture of the protein composed of the Gla domain (GD, blue), kringle-1 (K1, red), kringle-2 (K2, green), and protease domain (PD, gold) containing the binding site for the ligand FPR (arrow).