page_title: Lectin
hierarchical_section_title: Lectin
caption_attribution_description: Hemagglutinin. Ribbon diagram of hemagglutinin molecule. Source: The National Center for Biotechology Information. The National Center for Biotechology Information is a division of the National Library of Medicine, which is a division of the National Institutes of Health, which come under the jurisdiction of the US Department of Health and Human Services. Material made available by these institutions on line may be freely used as with all other US Federal government agencies. The NCBI runs several biomedical databases of enormous importance to doctors and scientists around the world. One of them is MMDB, a bank of "experimentally determined three-dimensional biomolecular structures." These are freely available on their website in an open access fashion. The NCBI places no restrictions on their access and use, except to ask that appropriate crediting is observed. The structures database consists of 3d video imagery of important proteins and other structures that can be visualized with Cn3D software. The above image is a still that I captured from one of the dozens of free files of Hemagglutinin. In this sense, this image is derivative. I hereby declare that I claim no copyright whatsoever over this image, for my part. As far as the source of the image is concerned, this was as stated released freely by the NCBI with no restriction on its use. I am placing the NIH and HHS tags below (there is no NCBI tag on Wikipedia yet).
context_page_description: Lectins are carbohydrate-binding proteins that are highly specific for sugar groups of other molecules and so cause agglutination of particular cells or precipitation of glycoconjugates and polysaccharides. Lectins have a role in recognition on the cellular and molecular level and play numerous roles in biological recognition phenomena involving cells, carbohydrates, and proteins. Lectins also mediate attachment and binding of bacteria, viruses, and fungi to their intended targets.
  Lectins are ubiquitous in nature and are found in many foods. Some foods, such as beans and grains, need to be cooked or fermented to reduce lectin content. Some lectins are beneficial, such as CLEC11A, which promotes bone growth, while others may be powerful toxins such as ricin.
  Lectins may be disabled by specific mono- and oligosaccharides, which bind to ingested lectins from grains, legumes, nightshade plants, and dairy; binding can prevent their attachment to the carbohydrates within the cell membrane. The selectivity of lectins means that they are useful for analyzing blood type, and they have been researched for potential use in genetically engineered crops to transfer pest resistance.
context_section_description: Lectins are carbohydrate-binding proteins that are highly specific for sugar groups of other molecules and so cause agglutination of particular cells or precipitation of glycoconjugates and polysaccharides. Lectins have a role in recognition on the cellular and molecular level and play numerous roles in biological recognition phenomena involving cells, carbohydrates, and proteins. Lectins also mediate attachment and binding of bacteria, viruses, and fungi to their intended targets.
  Lectins are ubiquitous in nature and are found in many foods. Some foods, such as beans and grains, need to be cooked or fermented to reduce lectin content. Some lectins are beneficial, such as CLEC11A, which promotes bone growth, while others may be powerful toxins such as   ricin.
  Lectins may be disabled by specific mono- and oligosaccharides, which bind to ingested lectins from grains, legumes, nightshade plants, and dairy; binding can prevent their attachment to the carbohydrates within the cell membrane. The selectivity of lectins means that they are useful for analyzing blood type, and they have been researched for potential use in genetically engineered crops to transfer pest resistance.
caption: Lateral hemagglutinine
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