![Fig. 5. Position of the L353R and G400D mutations in the structure of the fibrinogen Bβ chain. / (A) C-alpha trace of the AαBβγ trimer, outlining the position of Gly400 and Leu353, produced using the coordinates under the Protein Data Bank entry 1FZA. FGA, FGB, and FGG indicate the Aα, Bβ, and γ fibrinogen chains, respectively. N- and C-terminal residues of each chain are indicated. Light gray, black, and gray correspond to Aα, Bβ, and γ chains, respectively. (B) Multiple alignment of human, rat, bovine, xenopus, chicken, and lamprey fibrinogen Bβ chain in the region containing the 2 identified mutations. Identical amino acids are boxed. Positions of L353R and G400D mutations are indicated by arrows. Amino acid sequences were obtained from Swiss-Prot database (accession numbers: P02675 [human], P14480 [rat], P02676 [bovine], AAA85283 [xenopus], Q02020 [chicken], and FIBB_PETMA_2 [lamprey]) and numbered; the signal peptide is omitted. Secondary structures shown below the alignments (with cylinders representing α-helices and the arrow representing the β-strand) refer to the human protein, drawn from Spraggon et al2 data.](https://ash.silverchair-cdn.com/ash/content_public/journal/blood/95/4/10.1182_blood.v95.4.1336.004k16_1336_1341/6/bloo00416005y.jpeg?Expires=1735806375&Signature=Pg5vr103cgwYzLOge~V13SbESbuOpzqk85DIiIXbFsPAqGvZAtVvS-bjj9aJd4ysEAeZq4a0lfDukWJYxHgHy93hokebvhVJmLAY6c-zYjDmFrUJZSjJjeziidxdFe44SxgEelcPj5~cGWZ7M~28mXXfiqv5Rf8bKJmLk~y3SPiodSgNxGip9Eo3Tspn6CzwE7H7l9P9ndbgLqWuU64LOtoynZeQ5wGqAKwvvpV4PC59dDs5B91LiuK0CfZzWYIn~VXhYsTchtPxITxBBbqJNKu809JFrCsqcJLZ6yScdVnzq3V0z2NptsY5YmuKSEn66QXQYqa0i4KK~TNWm2dbFg__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA)
Position of the L353R and G400D mutations in the structure of the fibrinogen Bβ chain.
(A) C-alpha trace of the AαBβγ trimer, outlining the position of Gly400 and Leu353, produced using the coordinates under the Protein Data Bank entry 1FZA. FGA, FGB, and FGG indicate the Aα, Bβ, and γ fibrinogen chains, respectively. N- and C-terminal residues of each chain are indicated. Light gray, black, and gray correspond to Aα, Bβ, and γ chains, respectively. (B) Multiple alignment of human, rat, bovine, xenopus, chicken, and lamprey fibrinogen Bβ chain in the region containing the 2 identified mutations. Identical amino acids are boxed. Positions of L353R and G400D mutations are indicated by arrows. Amino acid sequences were obtained from Swiss-Prot database (accession numbers: P02675 [human], P14480 [rat], P02676 [bovine], AAA85283 [xenopus], Q02020 [chicken], and FIBB_PETMA_2 [lamprey]) and numbered; the signal peptide is omitted. Secondary structures shown below the alignments (with cylinders representing α-helices and the arrow representing the β-strand) refer to the human protein, drawn from Spraggon et al2 data.
