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.
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
