6TID
Structure of the N terminal domain of Bc2L-C lectin (1-131) in complex with H-type 1 antigen
This is a non-PDB format compatible entry.
Summary for 6TID
| Entry DOI | 10.2210/pdb6tid/pdb |
| Related PRD ID | PRD_900049 |
| Descriptor | Lectin, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | lectin, tnf-like, fucosylated antigen, sugar binding protein |
| Biological source | Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610) |
| Total number of polymer chains | 1 |
| Total formula weight | 14540.43 |
| Authors | Varrot, A.,Bermeo, R. (deposition date: 2019-11-22, release date: 2020-01-22, Last modification date: 2024-01-24) |
| Primary citation | Bermeo, R.,Bernardi, A.,Varrot, A. BC2L-C N-Terminal Lectin Domain Complexed with Histo Blood Group Oligosaccharides Provides New Structural Information. Molecules, 25:-, 2020 Cited by PubMed Abstract: Lectins mediate adhesion of pathogens to host tissues, filling in a key role in the first steps of infection. Belonging to the opportunistic pathogen , BC2L-C is a superlectin with dual carbohydrate specificity, believed to mediate cross-linking between bacteria and host cells. Its C-terminal domain binds to bacterial mannosides while its N-terminal domain (BCL2-CN) recognizes fucosylated human epitopes. BC2L-CN presents a tumor necrosis factor alpha (TNF-) fold previously unseen in lectins with a novel fucose binding mode. We report, here, the production of a novel recombinant form of BC2L-CN (rBC2L-CN2), which allowed better protein stability and unprecedented co-crystallization with oligosaccharides. Isothermal calorimetry measurements showed no detrimental effect on ligand binding and data were obtained on the binding of Globo H hexasaccharide and l-galactose. Crystal structures of rBC2L-CN2 were solved in complex with two blood group antigens: H-type 1 and H-type 3 (Globo H) by X-ray crystallography. They provide new structural information on the binding site, of importance for the structural-based design of glycodrugs as new antimicrobials with antiadhesive properties. PubMed: 31936166DOI: 10.3390/molecules25020248 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.614 Å) |
Structure validation
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