This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator.
The aim i s to determine the molecular structure of fgl2 a protein (tetramer) which consists of 4 subunits of 110,000 D. The protein is a member of the fibrinogen family of proteins with 36% homology to the beta and gamma subunits of fibrinogen. Fgl2 has been implicated in the pathogenesis of allo and xenograft rejection, viral hepatitis and cytokine induced fetal loss syndrome. It has prothrombinase activity which is attributable to a serine residue at position 89. The protein consists of two domains : The carboxy terminus is globular and has similaritiy to fibrinogen. Domain 2 is linear and contains the protease activity. We believe it is a transmembrane or membrane associated protein. Recent data has suggested that the globular carboxy domain binds to Fc gamma II receptors expressed on antigen presenting cells. Furthermore, fgl2 is expressed in Treg CD4+CD25+ FoxP3 cells and may account for their immunosuppressive activity. The project will be to define the structure of fgl2 and predict its binding domain and enzymatic motif.
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| Baker, Mariah R; Fan, Guizhen; Serysheva, Irina I (2015) Single-Particle Cryo-EM of the Ryanodine Receptor Channel in an Aqueous Environment. Eur J Transl Myol 25:4803 |
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