Title of article :
R-state Haemoglobin with Low Oxygen Affinity: Crystal Structures of Deoxy Human and Carbonmonoxy Horse Haemoglobin Bound to the Effector Molecule L35
Author/Authors :
Takeshi Yokoyama، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2006
Pages :
12
From page :
790
To page :
801
Abstract :
Although detailed crystal structures of haemoglobin (Hb) provide a clear understanding of the basic allosteric mechanism of the protein, and how this in turn controls oxygen affinity, recent experiments with artificial effector molecules have shown a far greater control of oxygen binding than with natural heterotropic effectors. Contrary to the established text-book view, these non-physiological compounds are able to reduce oxygen affinity very strongly without switching the protein to the T (tense) state. In an earlier paper we showed that bezafibrate (BZF) binds to a surface pocket on the α subunits of R state Hb, strongly reducing the oxygen affinity of this protein conformation. Here we report the crystallisation of Hb with L35, a related compound, and show that this binds to the central cavity of both R and T state Hb. The mechanism by which L35 reduces oxygen affinity is discussed, in relation to spectroscopic studies of effector binding.
Keywords :
bezafibrate derivative , Conformation , allosteric effector , X-ray crystallography
Journal title :
Journal of Molecular Biology
Serial Year :
2006
Journal title :
Journal of Molecular Biology
Record number :
1252591
Link To Document :
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