1b86
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(New page: 200px<br /> <applet load="1b86" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b86, resolution 2.5Å" /> '''HUMAN DEOXYHAEMOGLOB...)
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Revision as of 10:51, 8 November 2007
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HUMAN DEOXYHAEMOGLOBIN-2,3-DIPHOSPHOGLYCERATE COMPLEX
Overview
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.
About this Structure
1B86 is a Protein complex structure of sequences from Homo sapiens with DDH, HEM and DG2 as ligands. Full crystallographic information is available from OCA.
Reference
Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt structure at 2.5 A resolution., Richard V, Dodson GG, Mauguen Y, J Mol Biol. 1993 Sep 20;233(2):270-4. PMID:8377203
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Categories: Homo sapiens | Protein complex | Dodson, G.G. | Mauguen, Y. | Richard, V. | DDH | DG2 | HEM | 2 | 3-diphosphoglycerate | Allosteric effector | Haemoglobin