1buw
From Proteopedia
(New page: 200px<br /> <applet load="1buw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1buw, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF...) |
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==Overview== | ==Overview== | ||
Although numerous reports have documented that the S-nitrosylation of, cysteine residues by NO alters the activities of a wide variety of, proteins, the direct visualization and the structural consequences of this, reversible modification have not yet been reported for any protein. Here, we describe the crystal structure of S-nitroso-nitrosylhemoglobin, determined at a resolution of 1.8 A. The specific reaction of NO with, Cys93beta is confirmed in this structure, and a large, S-nitrosylation-induced change in the tertiary structure of the, COOH-terminal dipeptides of the beta subunits provides additional insight, into the stereochemical mechanism by which blood flow is regulated by the, interaction of NO with hemoglobin. | Although numerous reports have documented that the S-nitrosylation of, cysteine residues by NO alters the activities of a wide variety of, proteins, the direct visualization and the structural consequences of this, reversible modification have not yet been reported for any protein. Here, we describe the crystal structure of S-nitroso-nitrosylhemoglobin, determined at a resolution of 1.8 A. The specific reaction of NO with, Cys93beta is confirmed in this structure, and a large, S-nitrosylation-induced change in the tertiary structure of the, COOH-terminal dipeptides of the beta subunits provides additional insight, into the stereochemical mechanism by which blood flow is regulated by the, interaction of NO with hemoglobin. | ||
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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 and vasodilation]] | [[Category: oxygen transport and vasodilation]] | ||
| - | ''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 16:14:45 2007'' |
Revision as of 14:08, 12 November 2007
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CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A
Contents |
Overview
Although numerous reports have documented that the S-nitrosylation of, cysteine residues by NO alters the activities of a wide variety of, proteins, the direct visualization and the structural consequences of this, reversible modification have not yet been reported for any protein. Here, we describe the crystal structure of S-nitroso-nitrosylhemoglobin, determined at a resolution of 1.8 A. The specific reaction of NO with, Cys93beta is confirmed in this structure, and a large, S-nitrosylation-induced change in the tertiary structure of the, COOH-terminal dipeptides of the beta subunits provides additional insight, into the stereochemical mechanism by which blood flow is regulated by the, interaction of NO with hemoglobin.
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
1BUW is a Protein complex structure of sequences from Homo sapiens with HEM and NO as ligands. The following page contains interesting information on the relation of 1BUW with [Hemoglobin]. Full crystallographic information is available from OCA.
Reference
Crystal structure of the S-nitroso form of liganded human hemoglobin., Chan NL, Rogers PH, Arnone A, Biochemistry. 1998 Nov 24;37(47):16459-64. PMID:9843411
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