2. Academic Validation
  3. Hemoglobin: Structure, Function and Allostery

Hemoglobin: Structure, Function and Allostery

  • Subcell Biochem. 2020;94:345-382. doi: 10.1007/978-3-030-41769-7_14.
Mostafa H Ahmed 1,  Mohini S Ghatge 1 2,  Martin K Safo 3 4
Affiliations

Affiliations

  • 1 Department of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA, 23219, USA.
  • 2 Institute for Structural Biology, Drug Discovery and Development, Virginia Commonwealth University, Richmond, VA, 23219, USA.
  • 3 Department of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA, 23219, USA. [email protected].
  • 4 Institute for Structural Biology, Drug Discovery and Development, Virginia Commonwealth University, Richmond, VA, 23219, USA. [email protected].
PMID: 32189307 DOI: 10.1007/978-3-030-41769-7_14
Abstract

This chapter reviews how allosteric (heterotrophic) effectors and natural mutations impact hemoglobin (Hb) primary physiological function of oxygen binding and transport. First, an introduction about the structure of Hb is provided, including the ensemble of tense and relaxed Hb states and the dynamic equilibrium of Hb multistate. This is followed by a brief review of Hb variants with altered Hb structure and oxygen binding properties. Finally, a review of different endogenous and exogenous allosteric effectors of Hb is presented with particular emphasis on the atomic interactions of synthetic ligands with altered allosteric function of Hb that could potentially be harnessed for the treatment of diseases.

Keywords

Allosteric effectors; Allostery; Hemoglobin; Hemoglobin variants; Oxygen affinty; Relaxed state; T state; X-ray crystallography.

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Products
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    Product Name
    Description
    Target
    Research Area
  • HY-P2995
    Iron-containing Protein