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- Intelectins are lectins (carbohydrate-binding proteins) expressed in humans and other chordates. Humans express two types of intelectins encoded by ITLN1 and ITLN2 genes respectively. Several intelectins bind microbe-specific carbohydrate residues. Therefore, intelectins have been proposed to function as immune lectins. Even though intelectins contain fibrinogen-like domain found in the ficolins family of immune lectins, there is significant structural divergence. Thus, intelectins may not function through the same lectin-complement pathway. Most intelectins are still poorly characterized and they may have diverse biological roles. Human intelectin-1 (hIntL-1) has also been shown to bind lactoferrin, but the functional consequence has yet to be elucidated. Additionally, hIntL-1 is a major component of asthmatic mucus and may be involved in insulin physiology as well. (en)
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- 20382 (xsd:nonNegativeInteger)
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- Monomeric structure of XEEL-CRD with bound D-glycerol 1-phosphate. The protein is colored using a blue-red gradient from the N- to the C- terminus. Calcium ions are shown as green spheres and the coordinated water molecules are shown as red spheres. (en)
- Monomeric structure of human intelectin with bound allyl-beta-D-galactofuranose. The protein is colored using a blue-red gradient from the N- to the C- terminus. Calcium ions are shown as green spheres and the coordinated water molecules are shown as red spheres. (en)
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- 55600 (xsd:integer)
- 398574 (xsd:integer)
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- dbr:ITLN1
- Xenopus embryonic epidermal lectin (en)
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- Intelectins are lectins (carbohydrate-binding proteins) expressed in humans and other chordates. Humans express two types of intelectins encoded by ITLN1 and ITLN2 genes respectively. Several intelectins bind microbe-specific carbohydrate residues. Therefore, intelectins have been proposed to function as immune lectins. Even though intelectins contain fibrinogen-like domain found in the ficolins family of immune lectins, there is significant structural divergence. Thus, intelectins may not function through the same lectin-complement pathway. Most intelectins are still poorly characterized and they may have diverse biological roles. Human intelectin-1 (hIntL-1) has also been shown to bind lactoferrin, but the functional consequence has yet to be elucidated. Additionally, hIntL-1 is a major (en)
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