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Genetically crosslinked hemoglobin: a structural study.

Brucker EA
Acta Crystallogr D Biol Crystallogr 56 812-6 (2000)
Related entries: 1c7b, 1c7c

Cited: 15 times
EuropePMC logo PMID: 10930828

Abstract

The crystal structures of three recombinant human hemoglobins, rHb1. 0, rHb1.1 and rHb1.2, have been determined in the deoxy state at 1.8 A resolution. Two of the three proteins, rHb1.1 and rHb1.2, contain a genetic fusion of the alpha subunits, a one- or two-glycine link, respectively, whereas rHb1.0 does not. The glycine crosslinks, localized between one N- and C--termini pair of the alpha subunits in the deoxy crystalline state, do not perturb the overall tertiary or quaternary or even the local structure of hemoglobin. Therefore, genetic fusion to prevent the dissociation of the hemoglobin tetramer, thereby inhibiting renal clearance based upon molecular size, is a structurally conservative method to stabilize hemoglobin for use as an oxygen-delivery therapeutic.

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  2. Ion binding to biological macromolecules. Petukh M, Alexov E. Asian J Phys 23 735-744 (2014)
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  2. Exploring Oxidative Reactions in Hemoglobin Variants Using Mass Spectrometry: Lessons for Engineering Oxidatively Stable Oxygen Therapeutics. Strader MB, Alayash AI. Antioxid Redox Signal 26 777-793 (2017)

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  1. The RCSB Protein Data Bank: views of structural biology for basic and applied research and education. Rose PW, Prlić A, Bi C, Bluhm WF, Christie CH, Dutta S, Green RK, Goodsell DS, Westbrook JD, Woo J, Young J, Zardecki C, Berman HM, Bourne PE, Burley SK. Nucleic Acids Res 43 D345-56 (2015)
  2. Modulating distal cavities in the α and β subunits of human HbA reveals the primary ligand migration pathway. Birukou I, Maillett DH, Birukova A, Olson JS. Biochemistry 50 7361-7374 (2011)
  3. Blocking the gate to ligand entry in human hemoglobin. Birukou I, Soman J, Olson JS. J Biol Chem 286 10515-10529 (2011)
  4. Hemoglobin Kirklareli (α H58L), a New Variant Associated with Iron Deficiency and Increased CO Binding. Bissé E, Schaeffer-Reiss C, Van Dorsselaer A, Alayi TD, Epting T, Winkler K, Benitez Cardenas AS, Soman J, Birukou I, Samuel PP, Olson JS. J Biol Chem 292 2542-2555 (2017)
  5. Probing the conformation of hemoglobin presbyterian in the R-state. Acharya SA, Malavalli A, Peterson E, Sun PD, Ho C, Prabhakaran M, Arnone A, Manjula BN, Friedman JM. J Protein Chem 22 221-230 (2003)
  6. Protein-based blood substitutes: recent attempts at controlling pro-oxidant reactivity with and beyond hemoglobin. Scurtu VF, Moţ AC, Silaghi-Dumitrescu R. Pharmaceuticals (Basel) 6 867-880 (2013)
  7. Monodisperse 130 kDa and 260 kDa Recombinant Human Hemoglobin Polymers as Scaffolds for Protein Engineering of Hemoglobin-Based Oxygen Carriers. Marquardt DA, Doyle MP, Davidson JS, Epp JK, Aitken JF, Lemon DD, Anthony-Cahill SJ. J Funct Biomater 3 61-78 (2012)


Related citations provided by authors (2)

  1. Structures of a Hemoglobin-Based Blood Substitute: Insights Into the Function of Allosteric Proteins. Kroeger KS, Kundrot CE Structure 5 227-237 (1997)
  2. A Human Recombinant Haemoglobin Designed for Use as a Blood Substitute. Looker D, Abbot-Brown D, Cozart P, Durfee S, Hoffman S, Mathews AJ, Miller-Roehrich J, Shoemaker S, Trimble S, Fermi G, Komiyama NH, Nagai K, Stetler GL Nature 356 258-260 (1992)

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