PDBsum entry 3m3c

Hydrolase

PDB id: 3m3c

Contents

Protein chains

159 a.a. *

Ligands

A2G-GAL ×2

NPO ×2

SO4

Waters ×264

* Residue conservation analysis

PDB id:

3m3c

Name:

Hydrolase

Title:

Crystal structure of agrocybe aegerita lectin aal complexed with p- nitrophenyl tf disaccharide

Structure:

Anti-tumor lectin. Chain: a, b. Synonym: aal. Engineered: yes

Source:

Agrocybe aegerita. Black poplar mushroom. Organism_taxid: 5400. Gene: aal. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.188 R-free: 0.221

Authors:

L.Feng,D.Li,D.Wang

Key ref:

L.Feng et al. (2010). Structural insights into the recognition mechanism between an antitumor galectin AAL and the Thomsen-Friedenreich antigen. Faseb J, 24, 3861-3868. PubMed id: 20530247

Date:

09-Mar-10 Release date: 01-Dec-10

Protein chains

Q6WY08  (ATLE_CYCAE) -  Anti-tumor lectin (Fragment) from Cyclocybe aegerita

Seq: 158 a.a.

Struc: 159 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.1.21.- - ?????

Faseb J 24:3861-3868 (2010)

PubMed id: 20530247

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

L.Feng, H.Sun, Y.Zhang, D.F.Li, D.C.Wang.

ABSTRACT

Thomsen-Friedenreich (TF) antigen, which plays an important role in the regulation of cancer cell proliferation, occurs in approximately 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 unique in a conservative (Glu-water-Arg-water) structural motif-based hydrogen bond network. Structure-based mutagenesis analysis further revealed the residues responsible for recognition specificity and binding affinity. Crystal structures of AAL complexed with two other TF-containing glycans showed that the unique TF recognition mode is kept intact, which may be commonly adopted in some cancer-related galectins. The finding provided the new target and approach for the antitumor drug design and relative strategy based on the AAL-TF recognition mode as a prototype model.-Feng, L., Sun, H., Zhang, Y., Li, D.-F., Wang, D.-C. Structural insights into the recognition mechanism between an antitumor galectin AAL and the Thomsen-Friedenreich antigen.