The main objective in this project is to study Gelsolin Family Proteins. The actin cytoskeleton is actually a sophisticated structure which executes an array of cellular functions such as: cytokinesis, chemotaxis, cell locomotion, signal transduction and apoptosis. A great number of proteins (ABPs) in the cell control the assembly and disassembly of actin filaments. You can find over One hundred sixty actin-binding proteins known, which with actin, make up roughly 25% of cellular protein. ABPs are categorized to many significant groups depending on their sequence identity and tasks. We have explained the crystal structure of ATP bound gelsolin. We have demonstrated that ATP binding includes the 2 halves of gelsolin by means of creating quite a few polar and hydrophobic contacts. Amino acid remains which constitute the ATP-binding sites in inactive gelsolin are vastly spread in the activated molecule, thus, ATP binding is interrupted on gelsolin activation. This means that joining of ATP may modulate the level of sensitivity of gelsolin to calcium ions.
Moreover, we have revealed that only 2 calcium ions are required to activate geloslin. We imagine that this domain 2 calcium ion and the 1 in domain Six take part in the first activation of gelsolin. The crystal structure of the activated adseverin C-terminus is very much like the C-terminus of gelsolin.
The structural basis of actin dynamics at the cell membrane
Cytoskeleton and pathology
Gelsolin family proteins
Discussion and future perspectives……
Source: Uppsala University Library
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