Lipocalin

Lipocalins are proteins that bind specific molecules and transported into the cell. They are found in virtually all living organisms and are involved in a number of important physiological processes. Their structure is similar to a funnel or cup. In this funnel water-insoluble substances can be absorbed, transported, after sealing with a lid-like molecular structure and docking with receptor proteins in the cells. The lipocalins include, for example, the retinol -binding protein ( RBP), which transport vitamin A. Other lipocalins contrast, transport of smell and taste factors or bind pigments.

The lipocalins belonging to the family of Calycine, consist of about 180 amino acids and are therefore relatively small. Their biochemical and structural properties, as well as the function are well characterized, and are characterized by the binding of small hydrophobic molecules that attachment to specific receptors on the cell surface and the formation of complexes with soluble macromolecules. The from the word elements' lίpos "(Greek for fat) and " kάlyks "/" calix " (Greek. / Lat. Chalice for ) composite name thus describes task and structure of lipocalins.

Of the lipocalins artificial anticalins are derived, similar recognize an antibody for a specific target molecule. They may be used for therapeutic purposes in medicine of interest since they are in principle suitable for similar applications, such as therapeutic antibodies.

Lipocalins typically have twice orthogonally arranged beta-sheets, which form a coffee filter -like structure. This structure is referred to in the Bioinformatics and beta - sandwich. In the filter bag of non- covalently bound to hydrophobic molecules such as lipids, steroids, fragrances, bile acids, or retinoic acid derivatives. Previously known only from the associated with the lipocalins prostaglandin D synthase in that it also has an enzymatic activity.