2d5z: Difference between revisions
New page: left|200px<br /> <applet load="2d5z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d5z, resolution 1.45Å" /> '''Crystal structure o... |
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==Overview== | ==Overview== | ||
Although detailed crystal structures of haemoglobin (Hb) provide a clear, understanding of the basic allosteric mechanism of the protein, and how, this in turn controls oxygen affinity, recent experiments with artificial, effector molecules have shown a far greater control of oxygen binding than, with natural heterotropic effectors. Contrary to the established text-book, view, these non-physiological compounds are able to reduce oxygen affinity, very strongly without switching the protein to the T (tense) state. In an, earlier paper we showed that bezafibrate (BZF) binds to a surface pocket, on the alpha subunits of R state Hb, strongly reducing the oxygen affinity, of this protein conformation. Here we report the crystallisation of Hb, with L35, a related compound, and show that this binds to the central, cavity of both R and T state Hb. The mechanism by which L35 reduces oxygen, affinity is discussed, in relation to spectroscopic studies of effector, binding. | Although detailed crystal structures of haemoglobin (Hb) provide a clear, understanding of the basic allosteric mechanism of the protein, and how, this in turn controls oxygen affinity, recent experiments with artificial, effector molecules have shown a far greater control of oxygen binding than, with natural heterotropic effectors. Contrary to the established text-book, view, these non-physiological compounds are able to reduce oxygen affinity, very strongly without switching the protein to the T (tense) state. In an, earlier paper we showed that bezafibrate (BZF) binds to a surface pocket, on the alpha subunits of R state Hb, strongly reducing the oxygen affinity, of this protein conformation. Here we report the crystallisation of Hb, with L35, a related compound, and show that this binds to the central, cavity of both R and T state Hb. The mechanism by which L35 reduces oxygen, affinity is discussed, in relation to spectroscopic studies of effector, binding. | ||
==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: l35]] | [[Category: l35]] | ||
''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 21:26:30 2007'' | ||
