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. 1997 Apr 29;94(9):4366–4371. doi: 10.1073/pnas.94.9.4366

Figure 2.

Figure 2

MBP undergoes a large conformational change upon ligand binding. This involves a relative rearrangement of large rigid subdomains (I and II) best described as a combined hinge-twist movement. The maltose-binding site is formed by the interface between the two subdomains. The shaded spheres (A–D) indicate the regions that are predicted to be allosterically linked to maltose binding.