Comparison of properties of tumor necrosis factor-alpha converting enzyme (TACE) and some matrix metalloproteases (MMPs) in catalytic domains.
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.
Zhao
Yunbin
Y
Department of Chemistry, Huazhong University of Science and Technology, Wuhan 430074, China.
Feng
Wenfang
W
Yang
Yuzhen
Y
Ling
Lunjiang
L
Chen
Runsheng
R
D051722:ADAM Proteins / Q000737:chemistry*; D000072198:ADAM17 Protein; D020134:Catalytic Domain; D006801:Humans; D020782:Matrix Metalloproteinases / Q000737:chemistry*
D051722:ADAM Proteins; D020782:Matrix Metalloproteinases; D000072198:ADAM17 Protein; C000606462:ADAM17 protein, human