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The heparin‐binding site(s) of histidine‐rich glycoprotein as suggested by sequence homology with antithrombin III
Author(s) -
Koide Takehiko,
Foster Donald,
Odani Shoji
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80092-8
Subject(s) - histidine , antithrombin , heparin , binding site , homology (biology) , arginine , peptide sequence , glycoprotein , biochemistry , residue (chemistry) , amino acid , chemistry , consensus sequence , sequence (biology) , biology , gene
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 HI 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.