Fibrinogen beta chain

PDB rendering based on 1fza.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1FZA, 1FZB, 1FZC, 1FZE, 1FZF, 1FZG, 1LT9, 1LTJ, 1N86, 1N8E, 1RE3, 1RE4, 1RF0, 1RF1, 2A45, 2FFD, 2H43, 2HLO, 2HOD, 2HPC, 2OYH, 2OYI, 2Q9I, 2XNX, 2XNY, 2Z4E, 3BVH, 3E1I, 3GHG, 3H32, 3HUS

Identifiers

Symbols

FGB ; HEL-S-78p

External IDs

OMIM: 134830 MGI: 99501 HomoloGene: 3772 ChEMBL: 2048 GeneCards: FGB Gene

Gene ontology
Molecular function	• receptor binding • structural molecule activity • protein binding • protein binding, bridging • cell adhesion molecule binding • chaperone binding
Cellular component	• extracellular region • fibrinogen complex • extracellular space • plasma membrane • cell cortex • external side of plasma membrane • cell surface • platelet alpha granule • platelet alpha granule lumen • extracellular exosome • blood microparticle • extracellular vesicle
Biological process	• adaptive immune response • platelet degranulation • cell-matrix adhesion • signal transduction • blood coagulation • platelet activation • extracellular matrix organization • plasminogen activation • positive regulation of heterotypic cell-cell adhesion • fibrinolysis • induction of bacterial agglutination • cellular protein complex assembly • cellular response to leptin stimulus • innate immune response • positive regulation of vasoconstriction • positive regulation of exocytosis • positive regulation of protein secretion • protein polymerization • response to calcium ion • positive regulation of ERK1 and ERK2 cascade • platelet aggregation • cellular response to interleukin-1 • blood coagulation, fibrin clot formation • positive regulation of peptide hormone secretion • positive regulation of substrate adhesion-dependent cell spreading • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors • negative regulation of endothelial cell apoptotic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
154.56 – 154.57 Mb

Chr 3:
83.04 – 83.05 Mb

PubMed search

Fibrinogen beta chain, also known as FGB, is a gene found in humans and most other vertebrates with a similar system of blood coagulation.

The protein encoded by this gene is the beta component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.^[1]

Interactions

Fibrinogen beta chain has been shown to interact with Lipoprotein(a).^[2]

References

↑ "Entrez Gene: FGB fibrinogen beta chain".
↑ Klose, R; Fresser F; Kochl S; Parson W; Kapetanopoulos A; Fruchart-Najib J; Baier G; Utermann G (December 2000). "Mapping of a minimal apolipoprotein(a) interaction motif conserved in fibrin(ogen) beta - and gamma -chains". J. Biol. Chem. (UNITED STATES) 275 (49): 38206–12. doi:10.1074/jbc.M003640200. ISSN 0021-9258. PMID 10980194.

Doolittle RF (1984). "Fibrinogen and fibrin.". Annu. Rev. Biochem. 53: 195–229. doi:10.1146/annurev.bi.53.070184.001211. PMID 6383194.
Vasse M, Paysant J, Soria J; et al. (1997). "Regulation of fibrinogen biosynthesis by cytokines, consequences on the vascular risk.". Haemostasis. 26 Suppl 4: 331–9. doi:10.1159/000217313. PMID 8979138.
Herrick S, Blanc-Brude O, Gray A, Laurent G (1999). "Fibrinogen.". Int. J. Biochem. Cell Biol. 31 (7): 741–6. doi:10.1016/S1357-2725(99)00032-1. PMID 10467729.
Redman CM, Xia H (2001). "Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion.". Ann. N. Y. Acad. Sci. 936: 480–95. doi:10.1111/j.1749-6632.2001.tb03535.x. PMID 11460506.
Brennan SO, Fellowes AP, George PM (2001). "Molecular mechanisms of hypo- and afibrinogenemia.". Ann. N. Y. Acad. Sci. 936: 91–100. doi:10.1111/j.1749-6632.2001.tb03496.x. PMID 11460528.
Everse SJ (2003). "New insights into fibrin (ogen) structure and function.". Vox Sang. 83 Suppl 1: 375–82. doi:10.1111/j.1423-0410.2002.tb05338.x. PMID 12617173.
Scott EM, Ariëns RA, Grant PJ (2005). "Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease.". Arterioscler. Thromb. Vasc. Biol. 24 (9): 1558–66. doi:10.1161/01.ATV.0000136649.83297.bf. PMID 15217804.
Lord ST (2007). "Fibrinogen and fibrin: scaffold proteins in hemostasis.". Curr. Opin. Hematol. 14 (3): 236–41. doi:10.1097/MOH.0b013e3280dce58c. PMID 17414213.
Chen XC, Xu MT, Zhou W; et al. (2007). "A meta-analysis of relationship between beta-fibrinogen gene -148C/T polymorphism and susceptibility to cerebral infarction in Han Chinese.". Chin. Med. J. 120 (13): 1198–202. PMID 17637253.
Tarakhovskiĭ IuS, Galushchenko IV, Boroviagin VL; et al. (1979). "[Temperature-dependent changes in the profile of the sarcoplasmic reticulum membrane hydrophobic zones]". Biokhimiia 44 (5): 897–902. PMID 156564.
Watt KW, Takagi T, Doolittle RF (1979). "Amino acid sequence of the beta chain of human fibrinogen.". Biochemistry 18 (1): 68–76. doi:10.1021/bi00568a011. PMID 420779.
Gårdlund B, Hessel B, Marguerie G; et al. (1977). "Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments.". Eur. J. Biochem. 77 (3): 595–610. doi:10.1111/j.1432-1033.1977.tb11704.x. PMID 891553.
Blombäck B, Hessel B, Hogg D (1976). "Disulfide bridges in nh2 -terminal part of human fibrinogen.". Thromb. Res. 8 (5): 639–58. doi:10.1016/0049-3848(76)90245-0. PMID 936108.
Koopman J, Haverkate F, Grimbergen J; et al. (1992). "Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes.". Proc. Natl. Acad. Sci. U.S.A. 89 (8): 3478–82. doi:10.1073/pnas.89.8.3478. PMC 48891. PMID 1565641.
Koopman J, Haverkate F, Lord ST; et al. (1992). "Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala----Thr.". J. Clin. Invest. 90 (1): 238–44. doi:10.1172/JCI115841. PMC 443086. PMID 1634610.
Wu C, Chung AE (1991). "Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen A alpha and B beta chains.". J. Biol. Chem. 266 (28): 18802–7. PMID 1680863.
Yoshida N, Wada H, Morita K; et al. (1991). "A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine.". Blood 77 (9): 1958–63. PMID 2018836.
Chung DW, Harris JE, Davie EW (1991). "Nucleotide sequences of the three genes coding for human fibrinogen.". Adv. Exp. Med. Biol. 281: 39–48. doi:10.1007/978-1-4615-3806-6_3. PMID 2102623.
Danishefsky K, Hartwig R, Banerjee D, Redman C (1990). "Intracellular fate of fibrinogen B beta chain expressed in COS cells.". Biochim. Biophys. Acta 1048 (2–3): 202–8. doi:10.1016/0167-4781(90)90057-9. PMID 2322576.
Berg K, Kierulf P (1989). "DNA polymorphisms at fibrinogen loci and plasma fibrinogen concentration". Clin. Genet. 36 (4): 229–35. doi:10.1111/j.1399-0004.1989.tb03195.x. PMID 2572363.

PDB gallery

1fza: CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D

1fzb: CRYSTAL STRUCTURE OF CROSSLINKED FRAGMENT D

1fzc: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH TWO DIFFERENT BOUND LIGANDS

1fze: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN

1fzf: CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE

1fzg: CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE

1lt9: Crystal Structure of Recombinant Human Fibrinogen Fragment D

1ltj: Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands Gly-Pro-Arg-Pro-Amide and Gly-His-Arg-Pro-Amide

1n86: Crystal structure of human D-dimer from cross-linked fibrin complexed with GPR and GHRPLDK peptide ligands.

1n8e: Fragment Double-D from Human Fibrin

1re3: Crystal Structure of Fragment D of BbetaD398A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide

1re4: Crystal Structure of Fragment D of BbetaD398A Fibrinogen

1rf0: Crystal Structure of Fragment D of gammaE132A Fibrinogen

1rf1: Crystal Structure of Fragment D of gammaE132A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-amide

2a45: Crystal structure of the complex between thrombin and the central ""E"" region of fibrin

2ffd: Fibrinogen Fragment D with ""A"" knob peptide mimic GPRVVE

2h43: Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide

2hod: Crystal Structure of Fragment D from Human Fibrinogen Complexed with Gly-hydroxyPro-Arg-Pro-amide

2hpc: Crystal structure of fragment D from Human Fibrinogen Complexed with Gly-Pro-Arg-Pro-amide.

2oyh: Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide

2oyi: Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-Pro-Arg-Pro-Amide

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Fibrinogen beta chain

Interactions

See also

References

Further reading