Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2.

@article{Maskos2007FlexibilityAV,
  title={Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2.},
  author={Klaus Maskos and Ronggng Lang and Harald Tschesche and Wolfram Bode},
  journal={Journal of molecular biology},
  year={2007},
  volume={366 4},
  pages={
          1222-31
        }
}
The excessive activity of matrix metalloproteinases (MMPs) contributes to pathological processes such as arthritis, tumor growth and metastasis if not balanced by the tissue inhibitors of metalloproteinases (TIMPs). In arthritis, the destruction of fibrillar (type II) collagen is one of the hallmarks, with MMP-1 (collagenase-1) and MMP-13 (collagenase-3) being identified as key players in arthritic cartilage. MMP-13, furthermore, has been found in highly metastatic tumors. We have solved the 2… CONTINUE READING
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