%0 Journal Article
%T Homology modeling threedimensional structure of AnxB1 and reducing its immunogenicity by sequence-deleted mutagenesis
%A Yan Hongli
%A Song Yunlong
%A Liu Fan
%A He Yan
%A Sun Shuhan
%J Science China Life Sciences
%@ 1869-1889
%D 2004
%I 
%R 10.1360/03yc0085
%X AnxB1, a novel annexin previously isolated from Cysticercus cellulose, shows high thrombi affinity and anticoagulant activity in vivo. In order to investigate the relationship between structure and biological function, a predicted three-dimensional (3D) model of AnxB1 was generated by homology modeling. This model contains four homologous internal-domains and the C/ga trace of domain I, II and IV shows high similarity. Based on the structure characterization, four sequence-deleted mutants were constructed and expressed as GST fusion proteins in E. coli. Two of the mutants, GST-M3 and GST-M4 reserved high anticoagulant activity (p<0.01 vs. GST). Furthermore, compared with the wild type GST-AnxB1, the immunogenicity of GST-M3 and GST-M4 was reduced significantly (p<0.01) and the molecular weight was lowered to 27 kD and 34 kD, respectively. These observations laid a solid foundation for further study on developing new thrombolytic agents with higher efficiency and lower side effect.
%K annexin
%K homology modeling
%K sequence-deleted mutant
%K anticoagulant
%K immunogenicity
%U http://link.springer.com/article/10.1360/03yc0085