2d5x
From Proteopedia
(New page: 200px<br /> <applet load="2d5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d5x, resolution 1.45Å" /> '''Crystal structure o...) |
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| - | [[Image:2d5x.gif|left|200px]]<br /> | + | [[Image:2d5x.gif|left|200px]]<br /><applet load="2d5x" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2d5x, resolution 1.45Å" /> | caption="2d5x, resolution 1.45Å" /> | ||
'''Crystal structure of carbonmonoxy horse hemoglobin complexed with L35'''<br /> | '''Crystal structure of carbonmonoxy horse hemoglobin complexed with L35'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Although detailed crystal structures of haemoglobin (Hb) provide a clear | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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 HEM, CMO and L35 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Neya, S.]] | [[Category: Neya, S.]] | ||
| - | [[Category: Park, S | + | [[Category: Park, S Y.]] |
| - | [[Category: Tame, J | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:39 2008'' |
Revision as of 14:55, 21 February 2008
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Crystal structure of carbonmonoxy horse hemoglobin complexed with L35
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.
About this Structure
2D5X is a Protein complex structure of sequences from Equus caballus with , and as ligands. Full crystallographic information is available from OCA.
Reference
R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35., Yokoyama T, Neya S, Tsuneshige A, Yonetani T, Park SY, Tame JR, J Mol Biol. 2006 Feb 24;356(3):790-801. Epub 2005 Dec 21. PMID:16403522
Page seeded by OCA on Thu Feb 21 16:55:39 2008
Categories: Equus caballus | Protein complex | Neya, S. | Park, S Y. | Tame, J R. | Tsuneshige, A. | Yokoyama, T. | Yonetani, T. | CMO | HEM | L35 | Allosteric effector | Crystal structure | Hemoglobin
