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Crystal structure of a recombinant alphaEC domain from human fibrinogen-420.

Spraggon G, Applegate D, Everse SJ, Zhang JZ, Veerapandian L, Redman C, Doolittle RF, Grieninger G
Proc Natl Acad Sci U S A 95 9099-104 (1998)
Cited: 19 times
EuropePMC logo PMID: 9689040

Abstract

The crystal structure of a recombinant alphaEC domain from human fibrinogen-420 has been determined at a resolution of 2.1 A. The protein, which corresponds to the carboxyl domain of the alphaE chain, was expressed in and purified from Pichia pastoris cells. Felicitously, during crystallization an amino-terminal segment was removed, apparently by a contaminating protease, allowing the 201-residue remaining parent body to crystallize. An x-ray structure was determined by molecular replacement. The electron density was clearly defined, partly as a result of averaging made possible by there being eight molecules in the asymmetric unit related by noncrystallographic symmetry (P1 space group). Virtually all of an asparagine-linked sugar cluster is present. Comparison with structures of the beta- and gamma-chain carboxyl domains of human fibrinogen revealed that the binding cleft is essentially neutral and should not bind Gly-Pro-Arg or Gly-His-Arg peptides of the sort bound by those other domains. Nonetheless, the cleft is clearly evident, and the possibility of binding a carbohydrate ligand like sialic acid has been considered.

Articles - 1fzd mentioned but not cited (4)

  1. Crystal structure of a recombinant alphaEC domain from human fibrinogen-420. Spraggon G, Applegate D, Everse SJ, Zhang JZ, Veerapandian L, Redman C, Doolittle RF, Grieninger G. Proc Natl Acad Sci U S A 95 9099-9104 (1998)
  2. The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins. Chakraborty S, Rendón-Ramírez A, Ásgeirsson B, Dutta M, Ghosh AS, Oda M, Venkatramani R, Rao BJ, Dandekar AM, Goñi FM. F1000Res 2 286 (2013)
  3. Identification of potent aldose reductase inhibitors as antidiabetic (Anti-hyperglycemic) agents using QSAR based virtual Screening, molecular Docking, MD simulation and MMGBSA approaches. Bakal RL, Jawarkar RD, Manwar JV, Jaiswal MS, Ghosh A, Gandhi A, Zaki MEA, Al-Hussain S, Samad A, Masand VH, Mukerjee N, Nasir Abbas Bukhari S, Sharma P, Lewaa I. Saudi Pharm J 30 693-710 (2022)
  4. Sequence-based identification of amyloidogenic β-hairpins reveals a prostatic acid phosphatase fragment promoting semen amyloid formation. Heid LF, Agerschou ED, Orr AA, Kupreichyk T, Schneider W, Wördehoff MM, Schwarten M, Willbold D, Tamamis P, Stoldt M, Hoyer W. Comput Struct Biotechnol J 23 417-430 (2024)


Reviews citing this publication (9)

  1. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. Cereghino JL, Cregg JM. FEMS Microbiol Rev 24 45-66 (2000)
  2. Recombinant protein expression in Pichia pastoris. Cregg JM, Cereghino JL, Shi J, Higgins DR. Mol Biotechnol 16 23-52 (2000)
  3. Correlating structure and function during the evolution of fibrinogen-related domains. Doolittle RF, McNamara K, Lin K. Protein Sci 21 1808-1823 (2012)
  4. X-ray crystallographic studies on fibrinogen and fibrin. Doolittle RF. J Thromb Haemost 1 1559-1565 (2003)
  5. Structural basis of the fibrinogen-fibrin transformation: contributions from X-ray crystallography. Doolittle RF. Blood Rev 17 33-41 (2003)
  6. Crystal structure studies on fibrinogen and fibrin. Doolittle RF, Yang Z, Mochalkin I. Ann N Y Acad Sci 936 31-43 (2001)
  7. Fibrinogen splice variation and cross-linking: Effects on fibrin structure/function and role of fibrinogen γ' as thrombomobulin II. Duval C, Ariëns RAS. Matrix Biol 60-61 8-15 (2017)
  8. [Molecular mechanisms of the polymerization of fibrin and the formation of its three-dimensional network]. Lugovskoĭ EV, Gritsenko PG, Komisarenko SV. Bioorg Khim 35 437-456 (2009)
  9. New insights into fibrin (ogen) structure and function. Everse SJ. Vox Sang 83 Suppl 1 375-382 (2002)

Articles citing this publication (6)

  1. Fibrinogen triggers astrocyte scar formation by promoting the availability of active TGF-beta after vascular damage. Schachtrup C, Ryu JK, Helmrick MJ, Vagena E, Galanakis DK, Degen JL, Margolis RU, Akassoglou K. J Neurosci 30 5843-5854 (2010)
  2. Fibrinogen brescia: hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a gamma284 Gly-->Arg mutation. Brennan SO, Wyatt J, Medicina D, Callea F, George PM. Am J Pathol 157 189-196 (2000)
  3. A (1-->3)-beta-D-glucan recognition protein from the sponge Suberites domuncula. Mediated activation of fibrinogen-like protein and epidermal growth factor gene expression. Perović-Ottstadt S, Adell T, Proksch P, Wiens M, Korzhev M, Gamulin V, Müller IM, Müller WE. Eur J Biochem 271 1924-1937 (2004)
  4. The ultrastructure of fibrinogen-420 and the fibrin-420 clot. Mosesson MW, DiOrio JP, Hernandez I, Hainfeld JF, Wall JS, Grieninger G. Biophys Chem 112 209-214 (2004)
  5. Determining the crystal structure of fibrinogen. Doolittle RF. J Thromb Haemost 2 683-689 (2004)
  6. A genetic modifier of venous thrombosis in zebrafish reveals a functional role for fibrinogen AαE in early hemostasis. Freire C, Fish RJ, Vilar R, Di Sanza C, Grzegorski SJ, Richter CE, Shavit JA, Neerman-Arbez M. Blood Adv 4 5480-5491 (2020)


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