2d5x
From Proteopedia
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|PDB= 2d5x |SIZE=350|CAPTION= <scene name='initialview01'>2d5x</scene>, resolution 1.45Å | |PDB= 2d5x |SIZE=350|CAPTION= <scene name='initialview01'>2d5x</scene>, resolution 1.45Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=L35:2-[4-({[(3,5-DICHLOROPHENYL)AMINO]CARBONYL}AMINO)PHENOXY]-2-METHYLPROPANOIC+ACID'>L35</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2d5z|2D5Z]], [[2d60|2D60]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d5x OCA], [http://www.ebi.ac.uk/pdbsum/2d5x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d5x RCSB]</span> | ||
}} | }} | ||
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[[Category: Yokoyama, T.]] | [[Category: Yokoyama, T.]] | ||
[[Category: Yonetani, T.]] | [[Category: Yonetani, T.]] | ||
| - | [[Category: CMO]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: L35]] | ||
[[Category: allosteric effector]] | [[Category: allosteric effector]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
| Line 36: | Line 36: | ||
[[Category: l35]] | [[Category: l35]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:30:41 2008'' |
Revision as of 23:30, 30 March 2008
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| , resolution 1.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 2D5Z, 2D60
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 02:30:41 2008
