Structural insights into the recognition mechanism between an antitumor galectin AAL and the Thomsen-Friedenreich antigen.

ABSTRACT: Thomsen-Friedenreich (TF) antigen, which plays an important role in the regulation of cancer cell proliferation, occurs in ∼90% of all human cancers and precancerous conditions. Although TF antigen has been known for almost 80 yr as a pancarcinoma antigen, the recognition mechanism between TF antigen and target protein has not been structurally characterized. A number of studies indicated that TF disaccharide is a potential ligand of the galactoside-binding galectins. In this work, we identified the TF antigen as a potential ligand of the antitumor galectin AAL (Agrocybe aegerita lectin) through glycan array analysis and reported the crystal structure of AAL complexed with the TF antigen. The structure provides a first look at the recognition mode between AAL and TF antigen, which is uniqu

SUBMITTER: Feng L 

PROVIDER: S-EPMC3229422 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature