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.
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.
Intelectins are lectins (carbohydrate-binding proteins) expressed in humans and other chordates. Humans express two types of intelectins encoded by ITLN1 and ITLN2genes respectively.[1][2] Several intelectins bind microbe-specific carbohydrate residues. Therefore, intelectins have been proposed to function as immune lectins.[3][4] Even though intelectins contain fibrinogen-like domain found in the ficolins family of immune lectins, there is significant structural divergence.[5] 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,[6] but the functional consequence has yet to be elucidated. Additionally, hIntL-1 is a major component of asthmatic mucus[7] and may be involved in insulin physiology as well.[8]
^Yan J, Xu L, Zhang Y, Zhang C, Zhang C, Zhao F, Feng L (Oct 2013). "Comparative genomic and phylogenetic analyses of the intelectin gene family: implications for their origin and evolution". Developmental and Comparative Immunology. 41 (2): 189–99. doi:10.1016/j.dci.2013.04.016. PMID23643964.
^Suzuki YA, Shin K, Lönnerdal B (Dec 2001). "Molecular cloning and functional expression of a human intestinal lactoferrin receptor". Biochemistry. 40 (51): 15771–9. doi:10.1021/bi0155899. PMID11747454.
^Yang RZ, Lee MJ, Hu H, Pray J, Wu HB, Hansen BC, Shuldiner AR, Fried SK, McLenithan JC, Gong DW (Jun 2006). "Identification of omentin as a novel depot-specific adipokine in human adipose tissue: possible role in modulating insulin action". American Journal of Physiology. Endocrinology and Metabolism. 290 (6): E1253–61. doi:10.1152/ajpendo.00572.2004. PMID16531507.
