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- W1993128501 abstract "Coagulation factor IX-binding protein, isolated from Trimeresurus flavoviridis (IX-bp), is a C-type lectin-like protein. It is an anticoagulant consisting of homologous subunits, A and B. Each subunit has a Ca2+-binding site with a unique affinity (Kd values of 14 μM and 130 μM at pH 7.5). These binding characteristics are pH-dependent and, under acidic conditions, the Ca2+ binding of the low-affinity site was reduced considerably. In order to identify which site has high affinity and to investigate the pH-dependent Ca2+ release mechanism, we have determined the crystal structures of IX-bp at pH 6.5 and pH 4.6 (apo form), and compared the Ca2+-binding sites with each other and with those of the solved structures under alkaline conditions; pH 7.8 and pH 8.0 (complexed form). At pH 6.5, Glu43 in the Ca2+-binding site of subunit A displayed two conformations. One (minor) is that in the alkaline state, and the other (major) is that at pH 4.6. However, the corresponding Gln43 residue of subunit B is in only a single conformation, which is almost identical with that in the alkaline state. At pH 4.6, Glu43 of subunit A adopts a conformation similar to that of the major conformer observed at pH 6.5, while Gln43 of subunit B assumes a new conformation, and both Ca2+ positions are occupied by water molecules. These results showed that Glu43 of subunit A is much more sensitive to protonation than Gln43 of subunit B, and the conformational change of Glu43 occurs around pH 6.5, which may correspond to the step of Ca2+ release." @default.
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- W1993128501 date "2005-10-01" @default.
- W1993128501 modified "2023-09-26" @default.
- W1993128501 title "pH-Dependent Structural Changes at Ca2+-binding Sites of Coagulation Factor IX-binding Protein" @default.
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- W1993128501 doi "https://doi.org/10.1016/j.jmb.2005.08.018" @default.
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