Structure and domain-domain interactions of the gelatin binding site of human 72-kilodalton type IV collagenase (gelatinase A, matrix metalloproteinase 2).

@article{Bnyai1996StructureAD,
  title={Structure and domain-domain interactions of the gelatin binding site of human 72-kilodalton type IV collagenase (gelatinase A, matrix metalloproteinase 2).},
  author={L{\'a}szl{\'o} B{\'a}nyai and Hedvig Tordai and L Patthty},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 20},
  pages={12003-8}
}
We have shown previously that all three fibronectin type II modules of gelatinase A contribute to its gelatin affinity. In the present investigation we have studied the structure and module-module interactions of this gelatin-binding domain by circular dichroism spectroscopy and differential scanning calorimetry. Comparison of the Tm values of the thermal transitions of isolated type II modules with those of bimodular or trimodular proteins has shown that the second type II module is… CONTINUE READING