Molecular Interactions between Complement Factor H and Its Heparin and Heparan Sulfate Ligands.

ABSTRACT: Complement factor H (CFH) is the major regulator of the central complement protein C3b in the alternative pathway of complement activation. A molecular view of the CFH interaction with native heparan sulfate (HS) is central for understanding the mechanism of how surface-bound CFH interacts with C3b bound to host cell surfaces. HS is composed of sulfated heparin-like S-regions that alternate with desulfated NA-regions. Solution structural studies of heparin (equivalent to the S-regions) and desulfated HS (the NA-regions) by scattering and ultracentrifugation showed that each structure was mostly extended and partially bent, but with greater bending and flexibility in the NA-regions compared to the S-regions. Their solution structures have been deposited in the Protein Data Bank. The largest

SUBMITTER: Perkins SJ 

PROVIDER: S-EPMC3978290 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature