Lectin Collection

Ricin A-chain, artwork C017 / 3653
Ricin A-chain. Computer artwork showing the enzymatically active A-chain from a molecule of the toxic protein ricin. Ricin comprises two entwined amino acid chains; A (seen here) and B (not shown)

Ricin molecule, artwork C017 / 3652
Ricin molecule. Computer artwork showing the structure of a molecule of the toxic protein ricin. Ricin comprises two entwined amino acid chains; A (yellow) and B (blue)

Ricin molecule, artwork C017 / 3651
Ricin molecule. Computer artwork showing the structure of a molecule of the toxic protein ricin. Ricin comprises two entwined amino acid chains; A (yellow) and B (blue)

Ricin molecule, artwork C017 / 3650
Ricin molecule. Computer artwork showing the structure of a molecule of the toxic protein ricin. Ricin comprises two entwined amino acid chains; A (yellow) and B (blue)

Ricin A-chain, artwork C017 / 3654
Ricin A-chain. Computer artwork showing the enzymatically active A-chain from a molecule of the toxic protein ricin. Ricin comprises two entwined amino acid chains; A (seen here) and B (not shown)

Ricin molecule, artwork C017 / 3649
Ricin molecule. Computer artwork showing the structure of a molecule of the toxic protein ricin. Ricin comprises two entwined amino acid chains; A (yellow) and B (blue)

Concanavalin A F006 / 9668
Concanavalin A, molecular model. This lectin protein is found in legumes. Lectins are highly specific sugar-binding proteins that play a role in biological recognition

Lactose binding protein molecule F006 / 9629
Lactose binding protein. Molecular model of a lectin protein from the peanut plant (Arachis hypogaea) bound to a lactose molecule

Ricin molecule, artwork C017 / 3656
Ricin molecule. Computer artwork showing the structure of a molecule of the toxic protein ricin. Ricin comprises two entwined amino acid chains; A (yellow) and B (blue)

Ricin molecule, artwork C017 / 3655
Ricin molecule. Computer artwork showing the structure of a molecule of the toxic protein ricin. Ricin comprises two entwined amino acid chains; A (yellow) and B (blue)

Ricin molecule, artwork C017 / 3648
Ricin molecule Computer artwork showing the structure of a molecule of the toxic protein ricin (blue and yellow) with an active ribosome in the background

Plant agglutinin protein C015 / 6107
Plant agglutinin protein, molecular model. This example, from the hedge-apple (Maclura pomifera), is known as Maclura pomifera agglutinin (MPA). It is a tetrameric plant seed lectin

Plant agglutinin protein C015 / 6106
Plant agglutinin protein, molecular model. This example, from the hedge-apple (Maclura pomifera), is known as Maclura pomifera agglutinin (MPA). It is a tetrameric plant seed lectin

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"Lectin: Unveiling the Intricate World of Protein Interactions" In the realm of molecular biology, lectins stand as fascinating entities that captivate scientists worldwide. With their ability to bind specifically to certain carbohydrates, these proteins play a crucial role in various biological processes. Among them, Ricin A-chain takes center stage with its intricate structure and potent toxicity. Artworks C017/3653, C017/3652, C017/3651, and C017/3650 depict the awe-inspiring beauty of the Ricin molecule. Its complex arrangement showcases how nature crafts an elegant yet deadly weapon. The accompanying artwork C017/3654 zooms in on Ricin A-chain itself – a key player responsible for disrupting protein synthesis within cells. But they are not limited to ricin alone; Concanavalin A (F006/9668) and Lactose binding protein (F006/9629) also deserve recognition for their unique abilities. These captivating molecules exhibit specific carbohydrate-binding properties that have been extensively studied by researchers seeking to unravel their secrets. The remaining artworks - C017/3656, C017/3655, and C017/3648 - continue to showcase different facets of the enigmatic Ricin molecule's structure. Each image provides a glimpse into its complexity while leaving us marveling at nature's ingenuity. Lastly, Plant agglutinin protein (C015 / 6107) emerges as another intriguing member of the lectin family. This plant-derived protein possesses remarkable agglutination properties that enable it to clump together cells or particles—a phenomenon both mesmerizing and scientifically significant. As we delve deeper into understanding lectins' roles in cellular interactions and disease mechanisms, these captivating images serve as reminders of our ongoing quest for knowledge. Lectins hold immense potential for therapeutic applications or even unlocking new avenues in drug development.