1c7d: Difference between revisions
New page: left|200px<br /> <applet load="1c7d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c7d, resolution 1.80Å" /> '''DEOXY RHB1.2 (RECOM... |
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==Overview== | ==Overview== | ||
The crystal structures of three recombinant human hemoglobins, rHb1. 0, rHb1.1 and rHb1.2, have been determined in the deoxy state at 1.8 A, resolution. Two of the three proteins, rHb1.1 and rHb1.2, contain a, genetic fusion of the alpha subunits, a one- or two-glycine link, respectively, whereas rHb1.0 does not. The glycine crosslinks, localized, between one N- and C--termini pair of the alpha subunits in the deoxy, crystalline state, do not perturb the overall tertiary or quaternary or, even the local structure of hemoglobin. Therefore, genetic fusion to, prevent the dissociation of the hemoglobin tetramer, thereby inhibiting, renal clearance based upon molecular size, is a structurally conservative, method to stabilize hemoglobin for use as an oxygen-delivery therapeutic. | The crystal structures of three recombinant human hemoglobins, rHb1. 0, rHb1.1 and rHb1.2, have been determined in the deoxy state at 1.8 A, resolution. Two of the three proteins, rHb1.1 and rHb1.2, contain a, genetic fusion of the alpha subunits, a one- or two-glycine link, respectively, whereas rHb1.0 does not. The glycine crosslinks, localized, between one N- and C--termini pair of the alpha subunits in the deoxy, crystalline state, do not perturb the overall tertiary or quaternary or, even the local structure of hemoglobin. Therefore, genetic fusion to, prevent the dissociation of the hemoglobin tetramer, thereby inhibiting, renal clearance based upon molecular size, is a structurally conservative, method to stabilize hemoglobin for use as an oxygen-delivery therapeutic. | ||
==Disease== | |||
Known diseases associated with this structure: Erythremias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Erythremias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Erythrocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], HPFH, deletion type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Heinz body anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Heinz body anemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Heinz body anemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Hemoglobin H disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Hypochromic microcytic anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Methemoglobinemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Methemoglobinemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Sickle cell anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemia, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Thalassemia-beta, dominant inclusion-body OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Thalassemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: oxygen delivery vehicle]] | [[Category: oxygen delivery vehicle]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:17:55 2007'' | ||
Revision as of 17:11, 12 November 2007
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DEOXY RHB1.2 (RECOMBINANT HEMOGLOBIN)
OverviewOverview
The crystal structures of three recombinant human hemoglobins, rHb1. 0, rHb1.1 and rHb1.2, have been determined in the deoxy state at 1.8 A, resolution. Two of the three proteins, rHb1.1 and rHb1.2, contain a, genetic fusion of the alpha subunits, a one- or two-glycine link, respectively, whereas rHb1.0 does not. The glycine crosslinks, localized, between one N- and C--termini pair of the alpha subunits in the deoxy, crystalline state, do not perturb the overall tertiary or quaternary or, even the local structure of hemoglobin. Therefore, genetic fusion to, prevent the dissociation of the hemoglobin tetramer, thereby inhibiting, renal clearance based upon molecular size, is a structurally conservative, method to stabilize hemoglobin for use as an oxygen-delivery therapeutic.
DiseaseDisease
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 StructureAbout this Structure
1C7D is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. The following page contains interesting information on the relation of 1C7D with [Hemoglobin]. Full crystallographic information is available from OCA.
ReferenceReference
Genetically crosslinked hemoglobin: a structural study., Brucker EA, Acta Crystallogr D Biol Crystallogr. 2000 Jul;56(Pt 7):812-6. PMID:10930828
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