;Primary structure:<unk>  is an intracellular protein and, as such, does not contain the disulfide linkage between beta-strands B and F normally observed in the immunoglobulin constant domains. It does, however, contain two cysteine amino acid residues (Cys63 and Cys115) that are situated at structurally identical positions to those forming the disulfide linkage in the immunoglobulin constant domain. ;Secondary structure:<unk>  contains 154 amino acid residues, 103 of which were visible in the electron density map.<unk>  and the C-terminal domain of MLCK show amino acid sequence similarity to several quite unrelated muscle proteins such as titin or C-protein. The overall molecular fold of<unk>  consists of seven strands of antiparallel beta-pleated sheet that wrap around to form a barrel. There is also an extended tail of eight amino acid residues at the N terminus that does not participate in beta-sheet formation. The beta-barrel can be simply envisioned as two layers of beta-sheet, nearly parallel to one another, with one layer containing four and the other three beta-strands. ;Domains:<unk>  has a particular domain called Ig-like I-type (Immunoglobulin like intermediate type) with a length of 92 residues between 42 and 133. At the beginning it was thought that this domain was Ig- like C2-type but some studies determined that its structure shares characteristics from V-set and C2-set and that is why the a I-type was invented. These kind of domains mediates T-cell adhesion via its ectodomain, and signal transduction.
Telokin
Equilin
Reelin
Clathrin
Progerin
Retapamulin
Eribulin
Collectin