| 초록 |
Concanavalin A has been investigated for its ability to bind to pathogens. Due to the potential value of ConA to diagnostic microbiology, its mechanisms of action have been extensively studied; however, studies have reported different binding affinities due to the formation of different complexes. Monomeric structure of ConA can provide crucial information, as most reported structures are dimers or tetramers.We obtained a monomeric structure of ConA and revealed that metal coordination was a major cause of the carbohydrate-binding ability. When this structure was superimposed with apo-ConA, the conformational change in N14, a calcium-coordination residue, triggered other carbohydrate-binding residues. This result elucidates the mechanisms by which Ca2+ is crucial for sugar-binding while the elimination of Mn2+ would not affect sugar-binding. This study revealed the sequential mechanisms by which metal coordination affects sugar-binding residues. This analysis provides basic information for the controlling of ConA structure and a specific condition of crystallization indicates possible condition for the designing of diagnostic kit that can recognize pathogens, selectively. |
