Koide T, Foster D, Odani S
FEBS Lett. 1986 Jan 6;194(2):242-4. doi: 10.1016/0014-5793(86)80092-8.
A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located. The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. These observations strongly suggest that the heparin-binding sites of HRG and AT III are evolutionarily related. There was no apparent sequence similarity between the remaining about 70% portions of the two proteins.
在富含组氨酸的糖蛋白(HRG)的N端区域与抗凝血酶III(AT III)的N端区域之间发现了高度的序列同源性,而AT III的推定肝素结合位点就位于该区域。在HRG的同源序列中,与AT III的Arg-47相对应的、对肝素结合至关重要的氨基酸残基也是精氨酸(Arg 23和78)。这些观察结果有力地表明,HRG和AT III的肝素结合位点在进化上是相关的。这两种蛋白质其余约70%的部分之间没有明显的序列相似性。