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2d5x

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[[Image:2d5x.gif|left|200px]]
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[[Image:2d5x.png|left|200px]]
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{{STRUCTURE_2d5x| PDB=2d5x | SCENE= }}
{{STRUCTURE_2d5x| PDB=2d5x | SCENE= }}
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'''Crystal structure of carbonmonoxy horse hemoglobin complexed with L35'''
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===Crystal structure of carbonmonoxy horse hemoglobin complexed with L35===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16403522 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16403522}}
==About this Structure==
==About this Structure==
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[[Category: Hemoglobin]]
[[Category: Hemoglobin]]
[[Category: L35]]
[[Category: L35]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:45:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:59:33 2008''

Revision as of 19:59, 27 July 2008

Template:STRUCTURE 2d5x

Crystal structure of carbonmonoxy horse hemoglobin complexed with L35

Template:ABSTRACT PUBMED 16403522

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 Sun Jul 27 22:59:33 2008

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