Richard V, Dodson G G, Mauguen Y
Department of Chemistry, University of York Heslington, U.K.
J Mol Biol. 1993 Sep 20;233(2):270-4. doi: 10.1006/jmbi.1993.1505.
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.
利用从低盐溶液中生长的晶体，已在2.5埃分辨率下解析出血红蛋白-2,3-二磷酸甘油酸复合物的结构。结果显示，与阿诺内解析的先前的血红蛋白-2,3-二磷酸甘油酸高盐结构存在一些重要差异。首先，我们观察到结合位点对称性的丧失，其次，两个β82赖氨酸残基同时与2,3-二磷酸甘油酸相互作用，每个残基形成两个接触点。这种相互作用水平与在2,3-二磷酸甘油酸结合位点发生突变的天然血红蛋白突变体的功能行为一致。
