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Related Experiment Videos

Structure-function relationships in the low-affinity mutant haemoglobin Aalborg (Gly74 (E18)beta----Arg).

G Fermi1, M F Perutz, D Williamson

  • 1M.R.C. Laboratory of Molecular Biology, Cambridge, U.K.

Journal of Molecular Biology
|August 5, 1992
PubMed
Summary
This summary is machine-generated.

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Haemoglobin Aalborg, with an arginine substitution, shows reduced oxygen affinity and increased organic phosphate affinity due to an F helix shift. Haemoglobin Shepherds Bush, with an aspartate substitution, exhibits opposite effects.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Hemoglobin variants like Aalborg and Shepherds Bush exhibit altered oxygen binding and stability.
  • Understanding these alterations is crucial for diagnosing and treating hemoglobinopathies.

Purpose of the Study:

  • To elucidate the structural basis for the altered oxygen affinity and stability in Haemoglobin Aalborg and Shepherds Bush.
  • To compare the structural consequences of arginine (Aalborg) and aspartate (Shepherds Bush) substitutions at beta74(E18).

Main Methods:

  • X-ray crystallography to determine the 2.8 A resolution crystal structure of deoxyhaemoglobin Aalborg.
  • Structural comparison with deoxy- and oxyhaemoglobin A, and deoxyhaemoglobin Shepherds Bush.

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Main Results:

  • Haemoglobin Aalborg's Arg74(E18)beta protrudes from the heme pocket, donating hydrogen bonds and causing an F helix shift away from the EF-corner.
  • This F helix shift in Aalborg is opposite to that seen upon ligand binding and is linked to an increased tilt of the proximal histidine.
  • Asp74(E18)beta in Shepherds Bush is partially buried, potentially explaining its greater instability compared to Aalborg.

Conclusions:

  • The F helix shift in Haemoglobin Aalborg, influenced by steric and electrostatic effects of the arginine side-chain, likely accounts for its reduced oxygen affinity.
  • The opposing effects of arginine and aspartate substitutions on 2,3-diphosphoglycerate affinity can be explained by electrostatic interactions.