Lamin
As Lamine the type V intermediate filaments are known.
Lamins find in the cell nucleus of eukaryotic cells, where they are anchored by a plurality of membrane-bound proteins (eg Emerin ) to the inner nuclear membrane. As usual for intermediate filaments, lamins also have a tripartite domain structure. A relatively short head which leads into the conserved rod domain. It consists of four coiled-coil sections which are connected together by variable linker. The coiled coils have a characteristic Heptadenmuster, in which hydrophobic amino acid residues are in 1st and 4th position of a seven -amino acid portion. About this hydrophobic amino acids, the coiled-coil structure is formed. It squirm alphahelikale two protein strands around each other. In contrast to the cytoplasmic IF proteins of chordates the coil 1b domain of lamins is longer by 42 amino acids, a feature on all, including the cytoplasmic intermediate filaments of the protostomes (insects, nematodes, etc.) can be found. At the end of the rod domain of the tail ( tail ) domain follows. It is found in a nuclear localization signal, the box 105 (length 105 amino acids) and carboxy-terminal CAAX box. It is highly conserved, with the "C" is cysteine , "aa" for two aliphatic amino acids, and "X" represents any amino acid.
Interaction partners of lamins include the proteins LAP2alpha, Rb ( retinoblastoma protein), and BAF ( barrier -to- autointegration factor).