1gzx
OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS
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OverviewOverview
The cooperative binding of oxygen by haemoglobin results from restraints, on ligand binding in the T state. The unfavourable interactions made by, the ligands at the haems destabilise the T state and favour the high, affinity R state. The T <==> R equilibrium leads, in the presence of a, ligand, to a rapid increase in the R state population and therefore, generates cooperative binding. There is now considerable understanding of, this phenomenon, but the interactions that reduce ligand affinity in the T, state have not yet been fully explored, owing to the difficulties in, preparing T state haemoglobin crystals in which all the subunits are, oxygenated. A protocol has been developed to oxygenate deoxy T state adult, human haemoglobin (HbA) crystals in air at 4 C at all four haems ... [(full description)]
About this StructureAbout this Structure
1GZX is a [Protein complex] structure of sequences from [Homo sapiens] with HEM and OXY as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of T state haemoglobin with oxygen bound at all four haems., Paoli M, Liddington R, Tame J, Wilkinson A, Dodson G, J Mol Biol. 1996 Mar 8;256(4):775-92. PMID:8642597
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