1lft: Difference between revisions
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'''OXY HEMOGLOBIN (90% RELATIVE HUMIDITY)''' | {{Structure | ||
|PDB= 1lft |SIZE=350|CAPTION= <scene name='initialview01'>1lft</scene>, resolution 2.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''OXY HEMOGLOBIN (90% RELATIVE HUMIDITY)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LFT is a [ | 1LFT 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=1LFT OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12077435 12077435] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: t state]] | [[Category: t state]] | ||
''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 12:30:26 2008'' | ||
Revision as of 13:30, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
OXY HEMOGLOBIN (90% RELATIVE HUMIDITY)
OverviewOverview
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.
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
1LFT is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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