1xye: Difference between revisions
New page: left|200px<br /> <applet load="1xye" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xye, resolution 2.13Å" /> '''T-to-THigh Transiti... |
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==Overview== | ==Overview== | ||
Previous mutational studies on Tyr42alpha variants as well as the current, studies on the mutant hemoglobin alphaY42A show that the intersubunit, interactions associated with Tyr42alpha significantly stabilize the, alpha1beta2 interface of the quaternary-T deoxyhemoglobin tetramer., However, crystallographic studies, UV and visible resonance Raman, spectroscopy, CO combination kinetic measurements, and oxygen binding, measurements on alphaY42A show that the intersubunit interactions formed, by Tyr42alpha have only a modest influence on the structural properties, and ligand affinity of the deoxyhemoglobin tetramer. Therefore, the, alpha1beta2 interface interactions associated with Tyr42alpha do not, contribute significantly to the quaternary constraints that are, responsible for the low oxygen affinity of deoxyhemoglobin. The slight, increase in the ligand affinity of deoxy alphaY42A correlates with small, mutation-induced structural changes that perturb the environment of, Trp37beta, a critical region of the quaternary-T alpha1beta2 interface, that has been shown to be the major source of quaternary constraint in, deoxyhemoglobin. | Previous mutational studies on Tyr42alpha variants as well as the current, studies on the mutant hemoglobin alphaY42A show that the intersubunit, interactions associated with Tyr42alpha significantly stabilize the, alpha1beta2 interface of the quaternary-T deoxyhemoglobin tetramer., However, crystallographic studies, UV and visible resonance Raman, spectroscopy, CO combination kinetic measurements, and oxygen binding, measurements on alphaY42A show that the intersubunit interactions formed, by Tyr42alpha have only a modest influence on the structural properties, and ligand affinity of the deoxyhemoglobin tetramer. Therefore, the, alpha1beta2 interface interactions associated with Tyr42alpha do not, contribute significantly to the quaternary constraints that are, responsible for the low oxygen affinity of deoxyhemoglobin. The slight, increase in the ligand affinity of deoxy alphaY42A correlates with small, mutation-induced structural changes that perturb the environment of, Trp37beta, a critical region of the quaternary-T alpha1beta2 interface, that has been shown to be the major source of quaternary constraint in, deoxyhemoglobin. | ||
==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: hemoglobin mutant]] | [[Category: hemoglobin mutant]] | ||
''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 20:12:26 2007'' | ||
