Crystal structure of a cytocidal protein from lamprey and its mechanism of action in the selective killing of cancer cells.

ABSTRACT:

Background

In previous research, we found that lamprey immune protein (LIP) possessed cytocidal activity against tumor cells, but the mechanism of the selective recognition and killing of tumor cells by LIP was not identified.

Methods

Superresolution microscopy, crystallographic structural analysis, glycan chip assay, SPR experiments, FACS assays, computational studies and mass spectrometric analysis firmly establish the mode of action of LIP, which involves dual selective recognition and efficient binding.

Results

We determined the overall crystallographic structure of LIP at a resolution of 2.25 Å. LIP exhibits an elongated structure with dimensions of 105 Å × 30 Å × 30 Å containing an N-terminal lectin module and a C-terminal aerolysin module. Moreover, the Phe

SUBMITTER: Pang Y 

PROVIDER: S-EPMC6537362 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature