Human Hemoglobin Molecular Structure

Haemoglobin present in red blood cells is made up of 2 beta-globins (white) and two alpha-globin (blue) proteins. Sickle cell anaemia is a genetic disease where the body produces slightly stiff, crescent-shaped red blood cells which do not live as long as regular red blood cells. A single nucleotide mutation in the HBB gene causes the disease. The HBB gene is located on chromosome 11 and is involved for the production of beta-globin protein. The mutation alters the amino acid at residue 7 of the beta-globin protein. This mutation is highlighted in red on the molecular structure of human hemoglobin. The glutamic acid residue is replaced by a valine residue. The model was built using ChimeraX from X-ray diffraction crystal structure data in the Protein Data Bank (PDB ID 3NMM). 10.2210/pdb3NMM/pdb & https://www.cgl.ucsf.edu/chimerax/ ‘Blocking the gate to ligand entry in human hemoglobin.’ Birukou, I., Soman, J., Olson, J.S. (2011) J Biol Chem 286: 10515-10529 PubMed: 21193395 & DOI: 10.1074/jbc.M110.176271