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2d5x
From Proteopedia
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[[Image:2d5x.gif|left|200px]] | [[Image:2d5x.gif|left|200px]] | ||
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'''Crystal structure of carbonmonoxy horse hemoglobin complexed with L35''' | '''Crystal structure of carbonmonoxy horse hemoglobin complexed with L35''' | ||
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[[Category: Yokoyama, T.]] | [[Category: Yokoyama, T.]] | ||
[[Category: Yonetani, T.]] | [[Category: Yonetani, T.]] | ||
| - | [[Category: | + | [[Category: Allosteric effector]] |
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Hemoglobin]] |
| - | [[Category: | + | [[Category: L35]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:45:38 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:45, 3 May 2008
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. 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 Sat May 3 23:45:38 2008
