2d5z: Difference between revisions

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[[Image:2d5z.gif|left|200px]]<br />
[[Image:2d5z.gif|left|200px]]<br /><applet load="2d5z" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2d5z" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2d5z, resolution 1.45&Aring;" />
caption="2d5z, resolution 1.45&Aring;" />
'''Crystal structure of T-state human hemoglobin complexed with three L35 molecules'''<br />
'''Crystal structure of T-state human hemoglobin complexed with three L35 molecules'''<br />


==Overview==
==Overview==
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.
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.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
2D5Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HEM and L35 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D5Z OCA].  
2D5Z is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</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=2D5Z OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Neya, S.]]
[[Category: Neya, S.]]
[[Category: Park, S.Y.]]
[[Category: Park, S Y.]]
[[Category: Tame, J.R.]]
[[Category: Tame, J R.]]
[[Category: Tsuneshige, A.]]
[[Category: Tsuneshige, A.]]
[[Category: Yokoyama, T.]]
[[Category: Yokoyama, T.]]
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[[Category: l35]]
[[Category: l35]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:26:30 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:39 2008''

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