H-Gly-His-Arg-Pro-NH₂ |
| Katalog-Nr.GA22468 |
The central E region of fibrin contains two sets of polymerization knobs, A and B, that are cryptic in fibrinogen but become exposed after thrombin cleavage of fibrinopeptide A (FpA) and fibrinopeptide B (FpB) from the N-terminus of the Aα- and Bβ-chains, respectively. The location of the binding holes and possible models for knob-hole interactions are known from X-ray crystallographic studies using synthetic peptide analogs of knobs A and B. When fibrinogen fragment D and double-D are crystallized in the presence of both peptide analogs, the knob A peptide mimic H-Gly-Pro-Arg-Pro-NH? (GPRP-amide, H-1998) forms H-bond interactions with residues γ364Asp, γ330Asp, γ329Gln, and γ340His found in hole a. In the same manner, the knob B peptide mimic H-Gly-His-Arg-Pro-NH? (GHRP-amide, H-7318) interacts with residues Bβ397Glu, Bβ398Asp, and Bβ432Asp in hole b.
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Cas No.: 209623-54-1
Sample solution is provided at 25 µL, 10mM.
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The central E region of fibrin contains two sets of polymerization knobs, A and B, that are cryptic in fibrinogen but become exposed after thrombin cleavage of fibrinopeptide A (FpA) and fibrinopeptide B (FpB) from the N-terminus of the Aα- and B&
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