The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function.

@article{Grossman2010TheIP,
  title={The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function.},
  author={Moran Grossman and Dmitry Tworowski and Orly Dym and M H Lee and Yaakov Levy and Gillian Murphy and Irit Sagi},
  journal={Biochemistry},
  year={2010},
  volume={49 29},
  pages={6184-92}
}
Protein flexibility is thought to play key roles in numerous biological processes, including antibody affinity maturation, signal transduction, and enzyme catalysis, yet only limited information is available regarding the molecular details linking protein dynamics with function. A single point mutation at the distal site of the endogenous tissue inhibitor of metalloproteinase 1 (TIMP-1) enables this clinical target protein to tightly bind and inhibit membrane type 1 matrix metalloproteinase… CONTINUE READING