1n45: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
==Disease== | ==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> | [[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== | ==Function== | ||
Revision as of 04:29, 4 April 2013
X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEMEX-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME
Template:ABSTRACT PUBMED 10467099
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
1n45 is a 2 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1qq8. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Schuller DJ, Wilks A, Ortiz de Montellano PR, Poulos TL. Crystal structure of human heme oxygenase-1. Nat Struct Biol. 1999 Sep;6(9):860-7. PMID:10467099 doi:10.1038/12319
- ↑ 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