| Literature DB >> 8377203 |
V Richard1, G G Dodson, Y Mauguen.
Abstract
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.Entities:
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Year: 1993 PMID: 8377203 DOI: 10.1006/jmbi.1993.1505
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469