%A Wei Dong, Weiqin Lu, Wallace L. McKeehan, Yongde Luo, Sheng Ye %T Structural basis of heparan sulfate-specific degradation by heparinase III %0 Journal Article %D 2012 %J Protein Cell %J Protein & Cell %@ 1674-800X %R 10.1007/s13238-012-2056-z %P 950-961 %V 3 %N 12 %U {https://journal.hep.com.cn/pac/EN/10.1007/s13238-012-2056-z %8 2012-12-01 %X
Heparinase III (HepIII) is a 73-kDa polysaccharide lyase (PL) that degrades the heparan sulfate (HS) polysaccharides at sulfate-rare regions, which are important co-factors for a vast array of functional distinct proteins including the well-characterized antithrombin and the FGF/FGFR signal transduction system. It functions in cleaving metazoan heparan sulfate (HS) and providing carbon, nitrogen and sulfate sources for host microorganisms. It has long been used to deduce the structure of HS and heparin motifs; however, the structure of its own is unknown. Here we report the crystal structure of the HepIII from