1lfv
From Proteopedia
(New page: 200px<br /> <applet load="1lfv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lfv, resolution 2.80Å" /> '''OXY HEMOGLOBIN (88%...) |
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==Overview== | ==Overview== | ||
High-salt crystals of human oxy- and deoxyhaemoglobin have been studied at, different levels of environmental humidity and solvent content. The, structure of the oxy form remains relatively unchanged at all levels. The, deoxy form, however, undergoes a water-mediated transformation when the, relative humidity around the crystals is reduced below 93%. The space, group is maintained during the transformation, but the unit-cell volume, nearly doubles, with two tetrameric molecules in the asymmetric unit of, the low-humidity form compared with one in the native crystals., Interestingly, the haem geometry in the low-humidity form is closer to, that in the oxy form than to that in the native deoxy form. The quaternary, structure of one of the tetramers moves slightly towards that in the oxy, form, while that in the other is more different from the oxy form than, that in the high-salt native deoxy form. Thus, it would appear that, as in, the case of the liganded form, the deoxy form of haemoglobin can also, access an ensemble of related T states. | High-salt crystals of human oxy- and deoxyhaemoglobin have been studied at, different levels of environmental humidity and solvent content. The, structure of the oxy form remains relatively unchanged at all levels. The, deoxy form, however, undergoes a water-mediated transformation when the, relative humidity around the crystals is reduced below 93%. The space, group is maintained during the transformation, but the unit-cell volume, nearly doubles, with two tetrameric molecules in the asymmetric unit of, the low-humidity form compared with one in the native crystals., Interestingly, the haem geometry in the low-humidity form is closer to, that in the oxy form than to that in the native deoxy form. The quaternary, structure of one of the tetramers moves slightly towards that in the oxy, form, while that in the other is more different from the oxy form than, that in the high-salt native deoxy form. Thus, it would appear that, as in, the case of the liganded form, the deoxy form of haemoglobin can also, access an ensemble of related T states. | ||
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+ | ==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: t state]] | [[Category: t state]] | ||
- | ''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 18:00:01 2007'' |
Revision as of 15:53, 12 November 2007
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OXY HEMOGLOBIN (88% RELATIVE HUMIDITY)
Contents |
Overview
High-salt crystals of human oxy- and deoxyhaemoglobin have been studied at, different levels of environmental humidity and solvent content. The, structure of the oxy form remains relatively unchanged at all levels. The, deoxy form, however, undergoes a water-mediated transformation when the, relative humidity around the crystals is reduced below 93%. The space, group is maintained during the transformation, but the unit-cell volume, nearly doubles, with two tetrameric molecules in the asymmetric unit of, the low-humidity form compared with one in the native crystals., Interestingly, the haem geometry in the low-humidity form is closer to, that in the oxy form than to that in the native deoxy form. The quaternary, structure of one of the tetramers moves slightly towards that in the oxy, form, while that in the other is more different from the oxy form than, that in the high-salt native deoxy form. Thus, it would appear that, as in, the case of the liganded form, the deoxy form of haemoglobin can also, access an ensemble of related T states.
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
1LFV is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.
Reference
Structures of human oxy- and deoxyhaemoglobin at different levels of humidity: variability in the T state., Biswal BK, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1155-61. Epub 2002, Jun 20. PMID:12077435
Page seeded by OCA on Mon Nov 12 18:00:01 2007
Categories: Homo sapiens | Protein complex | Biswal, B.K. | Vijayan, M. | HEM | Environment | Hemoglobin | Humidity | T state