1ni6: Difference between revisions
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{{STRUCTURE_1ni6| PDB=1ni6 | SCENE= }} | {{STRUCTURE_1ni6| PDB=1ni6 | SCENE= }} | ||
===Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1=== | |||
{{ABSTRACT_PUBMED_12500973}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref> | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:012500973</ref><references group="xtra"/> | <ref group="xtra">PMID:012500973</ref><references group="xtra"/><references/> | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 00:05, 25 March 2013
Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1
Template:ABSTRACT PUBMED 12500973
DiseaseDisease
[HMOX1_HUMAN] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:614034]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.[1]
FunctionFunction
[HMOX1_HUMAN] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
About this StructureAbout this Structure
1ni6 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Lad L, Schuller DJ, Shimizu H, Friedman J, Li H, Ortiz de Montellano PR, Poulos TL. Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1. J Biol Chem. 2003 Mar 7;278(10):7834-43. Epub 2002 Dec 24. PMID:12500973 doi:http://dx.doi.org/10.1074/jbc.M211450200
- ↑ Yachie A, Niida Y, Wada T, Igarashi N, Kaneda H, Toma T, Ohta K, Kasahara Y, Koizumi S. Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency. J Clin Invest. 1999 Jan;103(1):129-35. PMID:9884342 doi:10.1172/JCI4165