2d5x: Difference between revisions
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[[Image:2d5x.gif|left|200px]] | [[Image:2d5x.gif|left|200px]] | ||
'''Crystal structure of carbonmonoxy horse hemoglobin complexed with L35''' | {{Structure | ||
|PDB= 2d5x |SIZE=350|CAPTION= <scene name='initialview01'>2d5x</scene>, resolution 1.45Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene> and <scene name='pdbligand=L35:2-[4-({[(3,5-DICHLOROPHENYL)AMINO]CARBONYL}AMINO)PHENOXY]-2-METHYLPROPANOIC ACID'>L35</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of carbonmonoxy horse hemoglobin complexed with L35''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2D5X is a [ | 2D5X is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5X OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16403522 16403522] | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: l35]] | [[Category: l35]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:23:38 2008'' | ||
Revision as of 17:23, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of carbonmonoxy horse hemoglobin complexed with L35
OverviewOverview
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 StructureAbout this Structure
2D5X is a Protein complex structure of sequences from Equus caballus. Full crystallographic information is available from OCA.
ReferenceReference
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
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