Summary
The crystal structural data of TACE, MMP-1, MMP-2, MMP-3 and MMP-9 were obtained from PDB database, and then their catalytic domains’ properties including conformation, molecular surface hydrophobicity and electrostatic potential were analyzed and compared by using Insight II molecular modeling software. It was found that the conformation and molecular surface hydrophobicity of catalytic domains of TACE and MMPs were not obviously different, but the molecular surface electrostatic potential of catalytic domain of TACE and MMPs had obvious differences. The findings are helpful in the Rational Drug Design of TACE selective inhibitor.
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This work was supported by a grant from the National Nature Science Foundation of China (Grants No.31371309).
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Zhao, Y., Feng, W., Yang, Y. et al. Comparison of properties of tumor necrosis factor-α converting enzyme (TACE) and some matrix metalloproteases (MMPs) in catalytic domains. J. Huazhong Univ. Sc. Technol. 26, 637–639 (2006). https://doi.org/10.1007/s11596-006-0601-9
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DOI: https://doi.org/10.1007/s11596-006-0601-9