1cmy: Difference between revisions
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==Overview== | ==Overview== | ||
Carbonmonoxy hemoglobin Ypsilanti (beta 99 Asp-Tyr) exhibits a quaternary, form distinctly different from any structures previously observed for, human hemoglobins. The relative orientation of alpha beta dimers in the, new quaternary form lies well outside the range of values observed for, normal unliganded and liganded tetramers (Baldwin, J., Chothia, C., J., Mol. Biol. 129:175-220, 1979). Despite this large quaternary structural, difference between carbonmonoxy hemoglobin Ypsilanti and the two canonical, structures, the new quaternary structure's hydrogen bonding interactions, in the "switch" region, and packing interactions in the "flexible joint", region, show noncovalent interactions characteristic of the alpha 1 beta 2, contacts of both unliganded and liganded normal hemoglobins. In contrast, to both canonical structures, the beta 97 histidine residue in, carbonmonoxy hemoglobin Ypsilanti is disengaged from quaternary packing, interactions that are generally believed to enforce two-state behavior in, ligand binding. These features of the new quaternary structure, denoted Y, may therefore be representative of quaternary states that occur, transiently along pathways between the normal unliganded, T, and liganded, R, hemoglobin structures. | Carbonmonoxy hemoglobin Ypsilanti (beta 99 Asp-Tyr) exhibits a quaternary, form distinctly different from any structures previously observed for, human hemoglobins. The relative orientation of alpha beta dimers in the, new quaternary form lies well outside the range of values observed for, normal unliganded and liganded tetramers (Baldwin, J., Chothia, C., J., Mol. Biol. 129:175-220, 1979). Despite this large quaternary structural, difference between carbonmonoxy hemoglobin Ypsilanti and the two canonical, structures, the new quaternary structure's hydrogen bonding interactions, in the "switch" region, and packing interactions in the "flexible joint", region, show noncovalent interactions characteristic of the alpha 1 beta 2, contacts of both unliganded and liganded normal hemoglobins. In contrast, to both canonical structures, the beta 97 histidine residue in, carbonmonoxy hemoglobin Ypsilanti is disengaged from quaternary packing, interactions that are generally believed to enforce two-state behavior in, ligand binding. These features of the new quaternary structure, denoted Y, may therefore be representative of quaternary states that occur, transiently along pathways between the normal unliganded, T, and liganded, R, hemoglobin structures. | ||
==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 transport]] | [[Category: oxygen transport]] | ||
''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 16:23:30 2007'' | ||
Revision as of 17:17, 12 November 2007
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THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN
OverviewOverview
Carbonmonoxy hemoglobin Ypsilanti (beta 99 Asp-Tyr) exhibits a quaternary, form distinctly different from any structures previously observed for, human hemoglobins. The relative orientation of alpha beta dimers in the, new quaternary form lies well outside the range of values observed for, normal unliganded and liganded tetramers (Baldwin, J., Chothia, C., J., Mol. Biol. 129:175-220, 1979). Despite this large quaternary structural, difference between carbonmonoxy hemoglobin Ypsilanti and the two canonical, structures, the new quaternary structure's hydrogen bonding interactions, in the "switch" region, and packing interactions in the "flexible joint", region, show noncovalent interactions characteristic of the alpha 1 beta 2, contacts of both unliganded and liganded normal hemoglobins. In contrast, to both canonical structures, the beta 97 histidine residue in, carbonmonoxy hemoglobin Ypsilanti is disengaged from quaternary packing, interactions that are generally believed to enforce two-state behavior in, ligand binding. These features of the new quaternary structure, denoted Y, may therefore be representative of quaternary states that occur, transiently along pathways between the normal unliganded, T, and liganded, R, hemoglobin structures.
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
1CMY is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The mutation beta 99 Asp-Tyr stabilizes Y--a new, composite quaternary state of human hemoglobin., Smith FR, Lattman EE, Carter CW Jr, Proteins. 1991;10(2):81-91. PMID:1896430
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