2d5x: Difference between revisions

[[Image:2d5x.gif|left|200px]]<br /><applet load="2d5x" size="350" color="white" frame="true" align="right" spinBox="true"  

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 alpha 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.

2D5X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=CMO:'>CMO</scene> and <scene name='pdbligand=L35:'>L35</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5X OCA].  

[[Category: Park, S Y.]]

[[Category: Tame, J R.]]

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