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. 2009 Sep 14;16(1):83. doi: 10.1186/1423-0127-16-83

Figure 1.

Figure 1

Schematic descriptions of the structure of the recombinant proteins and C peptide used in this work. Wild type human HMGB1 is composed of three domains: A box (amino acid residues 1-85), B boxes (amino acid residues 88-162) and a C-terminal acidic tail (amino acid residues 186-215). rHMGB1 is the full length recombinant human HMGB1. tHMGB1 is truncated HMGB1 lacking its C-terminal acidic tail. rHMGB1 A box or rHMGB1 B box is HMGB1 A box or B box fusioned with DHFR in order to stabilized express in prokaryotic system. C peptide is the C-terminal acidic tail composed of 30 amino acid residues. Eleven different deleted mutants lacking several amino acid residues in C-terminal acidic tail of HMGB1 are mHMGB1 -211-215, mHMGB1 - 206-215, mHMGB1 -201-215, mHMGB1 -196-215, mHMGB1 -191-215, mHMGB1 -186-200, mHMGB1 -196-210, mHMGB1 -196-205, mHMGB1 -198-207, mHMGB1 -201-210, and mHMGB1 -201-205. These mutants are recombinant human HMGB1 lacking amino acid residues 211-215, 206-215, 201-215, 196-215, 191-215, 186-200, 196-210, 196-205, 198-207, 201-210 and 201-205 respectively. The sprit shadow stands for the deleted regions.