The use of whole insect larvae as a source of recombinant proteins offers a more cost-effective method of producing large quantities of human proteins than conventional cell-culture approaches. Human carboxylesterase 1 has been produced in and isolated from whole Trichoplusia ni larvae. The recombinant protein was crystallized and its structure was solved to 2.2 resolution. The results indicate that the larvae-produced enzyme is essentially identical to that isolated from cultured Sf21 cells, supporting the use of this expression system to produce recombinant enzymes for crystallization studies.
Ligand
Representative scheme of Carb_B_Chordata structure and an image from PDBsum server
Databases
PDB-Sum
4AB1 Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
4AB1Fold classification based on Structure-Structure alignment of Proteins - FSSP server
