6hbw
From Proteopedia
(New page: 200px<br /> <applet load="6hbw" size="450" color="white" frame="true" align="right" spinBox="true" caption="6hbw, resolution 2.00Å" /> '''Crystal structure o...) |
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==Overview== | ==Overview== | ||
An atomic-level understanding of the interactions between hemoglobin, molecules that contribute to the formation of pathological fibers in, sickle cell disease remains elusive. By exploring crystal structures of, mutant hemoglobins with altered polymerization properties, insight can be, gained into sickle cell hemoglobin (HbS) polymerization. We present here, the 2.0-A resolution deoxy crystal structure of human hemoglobin mutated, to tryptophan at the beta6 position, the site of the glutamate --> valine, mutation in HbS. Unlike leucine and isoleucine, which promote, polymerization relative to HbS, tryptophan inhibits polymerization. Our, results provide explanations for the altered polymerization properties and, reveal a fundamentally different double strand that may provide a model, for interactions within a fiber and/or interactions leading to, heterogeneous nucleation. | An atomic-level understanding of the interactions between hemoglobin, molecules that contribute to the formation of pathological fibers in, sickle cell disease remains elusive. By exploring crystal structures of, mutant hemoglobins with altered polymerization properties, insight can be, gained into sickle cell hemoglobin (HbS) polymerization. We present here, the 2.0-A resolution deoxy crystal structure of human hemoglobin mutated, to tryptophan at the beta6 position, the site of the glutamate --> valine, mutation in HbS. Unlike leucine and isoleucine, which promote, polymerization relative to HbS, tryptophan inhibits polymerization. Our, results provide explanations for the altered polymerization properties and, reveal a fundamentally different double strand that may provide a model, for interactions within a fiber and/or interactions leading to, heterogeneous nucleation. | ||
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| + | ==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 23:52:41 2007'' |
Revision as of 21:46, 12 November 2007
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Crystal structure of deoxy-human hemoglobin beta6 glu->trp
Contents |
Overview
An atomic-level understanding of the interactions between hemoglobin, molecules that contribute to the formation of pathological fibers in, sickle cell disease remains elusive. By exploring crystal structures of, mutant hemoglobins with altered polymerization properties, insight can be, gained into sickle cell hemoglobin (HbS) polymerization. We present here, the 2.0-A resolution deoxy crystal structure of human hemoglobin mutated, to tryptophan at the beta6 position, the site of the glutamate --> valine, mutation in HbS. Unlike leucine and isoleucine, which promote, polymerization relative to HbS, tryptophan inhibits polymerization. Our, results provide explanations for the altered polymerization properties and, reveal a fundamentally different double strand that may provide a model, for interactions within a fiber and/or interactions leading to, heterogeneous nucleation.
Disease
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 Structure
6HBW is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of deoxy-human hemoglobin beta6 Glu --> Trp. Implications for the structure and formation of the sickle cell fiber., Harrington DJ, Adachi K, Royer WE Jr, J Biol Chem. 1998 Dec 4;273(49):32690-6. PMID:9830011
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