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• W2070484351 startingPage "4425" @default.
• W2070484351 abstract "Abstract Fibrinogen residue Bβ432Asp is part of hole “b” that interacts with knob “B,” whose sequence starts with Gly-His-Arg-Pro-amide (GHRP). Because previous studies showed BβD432A has normal polymerization, we hypothesized that Bβ432Asp is not critical for knob “B” binding and that new knob-hole interactions would compensate for the loss of this Asp residue. To test this hypothesis, we solved the crystal structure of fragment D from BβD432A. Surprisingly, the structure (rfD-BβD432A+GH) showed the peptide GHRP was not bound to hole “b.” We then re-evaluated the polymerization of this variant by examining clot turbidity, clot structure, and the rate of FXIIIa cross-linking. The turbidity and the rate of γ-γ dimer formation for BβD432A were indistinguishable compared with normal fibrinogen. Scanning electron microscopy showed no significant differences between the clots of BβD432A and normal, but the thrombin-derived clots had thicker fibers than clots obtained from batroxobin, suggesting that cleavage of FpB is more important than “B:b” interactions. We conclude that hole “b” and “B:b” knob-hole binding per se have no influence on fibrin polymerization." @default.
• W2070484351 created "2016-06-24" @default.
• W2070484351 creator A5011933651 @default.
• W2070484351 creator A5026633318 @default.
• W2070484351 date "2009-04-30" @default.
• W2070484351 modified "2023-09-30" @default.
• W2070484351 title "Fibrinogen variant BβD432A has normal polymerization but does not bind knob “B”" @default.
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• W2070484351 doi "https://doi.org/10.1182/blood-2008-09-178178" @default.
• W2070484351 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2676095" @default.
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