1aby
From Proteopedia
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| - | [[Image:1aby.gif|left|200px]] | + | [[Image:1aby.gif|left|200px]] |
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| - | '''CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)''' | + | {{Structure |
| + | |PDB= 1aby |SIZE=350|CAPTION= <scene name='initialview01'>1aby</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ABY is a [ | + | 1ABY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABY OCA]. |
==Reference== | ==Reference== | ||
| - | A human recombinant haemoglobin designed for use as a blood substitute., Looker D, Abbott-Brown D, Cozart P, Durfee S, Hoffman S, Mathews AJ, Miller-Roehrich J, Shoemaker S, Trimble S, Fermi G, et al., Nature. 1992 Mar 19;356(6366):258-60. PMID:[http:// | + | A human recombinant haemoglobin designed for use as a blood substitute., Looker D, Abbott-Brown D, Cozart P, Durfee S, Hoffman S, Mathews AJ, Miller-Roehrich J, Shoemaker S, Trimble S, Fermi G, et al., Nature. 1992 Mar 19;356(6366):258-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1552945 1552945] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''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 09:55:32 2008'' |
Revision as of 07:55, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)
Contents |
Overview
The need to develop a blood substitute is now urgent because of the increasing concern over blood-transmitted viral and bacterial pathogens. Cell-free haemoglobin solutions and human haemoglobin synthesized in Escherichia coli and Saccharomyces cerevisiae have been investigated as potential oxygen-carrying substitutes for red blood cells. But these haemoglobins cannot be used as a blood substitute because (1) the oxygen affinity in the absence of 2,3-bisphosphoglycerate is too high to allow unloading of enough oxygen in the tissues, and (2) they dissociate into alpha beta dimers that are cleared rapidly by renal filtration, which can result in long-term kidney damage. We have produced a human haemoglobin using an expression vector containing one gene encoding a mutant beta-globin with decreased oxygen affinity and one duplicated, tandemly fused alpha-globin gene. Fusion of the two alpha-globin subunits increases the half-life of this haemoglobin molecule in vivo by preventing its dissociation into alpha beta dimers and therefore also eliminates renal toxicity.
Disease
Known diseases associated with this structure: Erythremias, alpha- OMIM:[141800], Erythremias, beta- OMIM:[141900], Erythrocytosis OMIM:[141850], HPFH, deletion type OMIM:[141900], Heinz body anemia OMIM:[141850], Heinz body anemias, alpha- OMIM:[141800], Heinz body anemias, beta- OMIM:[141900], Hemoglobin H disease OMIM:[141850], Hypochromic microcytic anemia OMIM:[141850], Methemoglobinemias, alpha- OMIM:[141800], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia, alpha- OMIM:[141850], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, alpha- OMIM:[141800], Thalassemias, beta- OMIM:[141900]
About this Structure
1ABY is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A human recombinant haemoglobin designed for use as a blood substitute., Looker D, Abbott-Brown D, Cozart P, Durfee S, Hoffman S, Mathews AJ, Miller-Roehrich J, Shoemaker S, Trimble S, Fermi G, et al., Nature. 1992 Mar 19;356(6366):258-60. PMID:1552945
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