ArticleJournal of structural biology2016
Crystal structure of carbonmonoxy sickle hemoglobin in R-state conformation.
Article in Journal of structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Sphingosine-1-Phosphate Regulation to Alleviate Sickle Cell Disease Severity: A Promising Therapeutic Approach.Saudi medical journal · 2026Review
- Computational screening of phytochemicals present in some Nigerian medicinal plants against sickle cell disease.Scientific reports · 2024Article
- Biophysical chemistry behind sickle cell anemia and the mechanism of voxelotor action.Scientific reports · 2024Article
- Evaluating sheep hemoglobins with MD simulations as an animal model for sickle cell disease.Scientific reports · 2024Article
- Targeted modification of furan-2-carboxaldehydes into Michael acceptor analogs yielded long-acting hemoglobin modulators with dual antisickling activities.Chemical biology & drug design · 2024Article
- Quantitative assessment of the in-vitro binding kinetics of antisickling aromatic aldehydes with hemoglobin A: A universal HPLC-UV/Vis method to quantitate Schiff-base adduct formation.Journal of pharmaceutical and biomedical analysis · 2023Article
- X-ray crystallography and sickle cell disease drug discovery-a tribute to Donald Abraham.Frontiers in molecular biosciences · 2023Review
- Design, Synthesis, and Investigation of Novel Nitric Oxide (NO)-Releasing Aromatic Aldehydes as Drug Candidates for the Treatment of Sickle Cell Disease.Molecules (Basel, Switzerland) · 2022Article
- Metabolic Reprogramming in Sickle Cell Diseases: Pathophysiology and Drug Discovery Opportunities.International journal of molecular sciences · 2022Review
- Design, Synthesis, and Antisickling Investigation of a Nitric Oxide-Releasing Prodrug of 5HMF for the Treatment of Sickle Cell Disease.Biomolecules · 2022Article
- Molecular insight into 2-phosphoglycolate activation of the phosphatase activity of bisphosphoglycerate mutase.Acta crystallographica. Section D, Structural biology · 2022Article
- Modulating hemoglobin allostery for treatment of sickle cell disease: current progress and intellectual property.Expert opinion on therapeutic patents · 2022Review
- Plasma Levels of Acyl-Carnitines and Carboxylic Acids Correlate With Cardiovascular and Kidney Function in Subjects With Sickle Cell Trait.Frontiers in physiology · 2022Article
- Exploration of Structure-Activity Relationship of Aromatic Aldehydes Bearing Pyridinylmethoxy-Methyl Esters as Novel Antisickling Agents.Journal of medicinal chemistry · 2020Article
- VZHE-039, a novel antisickling agent that prevents erythrocyte sickling under both hypoxic and anoxic conditions.Scientific reports · 2020Article
- An Investigation of Structure-Activity Relationships of Azolylacryloyl Derivatives Yielded Potent and Long-Acting Hemoglobin Modulators for Reversing Erythrocyte Sickling.Biomolecules · 2020Article
- Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Hemoglobin: Structure, Function and Allostery.Sub-cellular biochemistry · 2020Review
- Rational Drug Design of Peptide-Based Therapies for Sickle Cell Disease.Molecules (Basel, Switzerland) · 2019Review
- Substitutions in the β subunits of sickle-cell hemoglobin improve oxidative stability and increase the delay time of sickle-cell fiber formation.The Journal of biological chemistry · 2019Article
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Authors and funding
8 authors.
Funding
Abstract
The fundamental pathophysiology of sickle cell disease is predicated by the polymerization of deoxygenated (T-state) sickle hemoglobin (Hb S) into fibers that distort red blood cells into the characteristic sickle shape. The crystal structure of deoxygenated Hb S (DeoxyHb S) and other studies suggest that the polymer is initiated by a primary interaction between the mutation βVal6 from one Hb S molecule, and a hydrophobic acceptor pocket formed by the residues βAla70, βPhe85 and βLeu88 of an adjacent located Hb S molecule. On the contrary, oxygenated or liganded Hb S does not polymerize or incorporate in the polymer. In this paper we present the crystal structure of carbonmonoxy-ligated sickle Hb (COHb S) in the quaternary classical R-state at 1.76Å. The overall structure and the pathological donor and acceptor environments of COHb S are similar to those of the isomorphous CO-ligated R-state normal Hb (COHb A), but differ significantly from DeoxyHb S as expected. More importantly, the packing of COHb S molecules does not show the typical pathological interaction between βVal6 and the βAla70, βPhe85 and βLeu88 hydrophobic acceptor pocket observed in DeoxyHb S crystal. The structural analysis of COHb S, COHb A and DeoxyHb S provides atomic level insight into why liganded hemoglobin does not form a polymer.
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