Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution.
The haemoglobin-2,3-diphosphoglycerate complex structure has been solved at 2.5 A resolution using crystals grown from low-salt solutions. The results show some important differences with the precedent haemoglobin-2,3-diphosphoglycerate high-salt structure solved by Arnone. First, we observe a loss of symmetry in the binding site, secondly both of the lysine residues 82 beta interact with 2,3-diphosphoglycerate at the same time, each making two contacts. This level of interaction is in agreement with the functional behaviour of natural haemoglobin mutants with mutations at the 2,3-diphosphoglycerate binding site.
Department of Chemistry, University of York Heslington, U.K.
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Richard
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Dodson
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Mauguen
D019794:2,3-Diphosphoglycerate; D000495:Allosteric Site; D000595:Amino Acid Sequence; D004163:Diphosphoglyceric Acids / Q000737:chemistry* / Q000378:metabolism; D005583:Fourier Analysis; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008961:Models, Structural; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction / Q000379:methods
D004163:Diphosphoglyceric Acids; D006454:Hemoglobins; C083289:deoxyhaemoglobin-2,3-diphosphoglycerate complex; D019794:2,3-Diphosphoglycerate