1lft: Difference between revisions

No edit summary
No edit summary
Line 4: Line 4:
|PDB= 1lft |SIZE=350|CAPTION= <scene name='initialview01'>1lft</scene>, resolution 2.60&Aring;
|PDB= 1lft |SIZE=350|CAPTION= <scene name='initialview01'>1lft</scene>, resolution 2.60&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1lfl|1LFL]], [[1lfq|1LFQ]], [[1lfv|1LFV]], [[1lfy|1LFY]], [[1lfz|1LFZ]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lft OCA], [http://www.ebi.ac.uk/pdbsum/1lft PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lft RCSB]</span>
}}
}}


Line 14: Line 17:
==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.
==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==
Line 27: Line 27:
[[Category: Biswal, B K.]]
[[Category: Biswal, B K.]]
[[Category: Vijayan, M.]]
[[Category: Vijayan, M.]]
[[Category: HEM]]
[[Category: environment]]
[[Category: environment]]
[[Category: hemoglobin]]
[[Category: hemoglobin]]
Line 33: Line 32:
[[Category: t state]]
[[Category: t state]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:30:26 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:02:17 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA