1s8c

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Template:STRUCTURE 1s8c

Contents 1 Crystal structure of human heme oxygenase in a complex with biliverdine 2 Disease 3 Function 4 About this Structure 5 See Also 6 Reference

Crystal structure of human heme oxygenase in a complex with biliverdine

Template:ABSTRACT PUBMED 15049686

Disease

[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]

Function

[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

1s8c is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Heme oxygenase

Reference

• Lad L, Friedman J, Li H, Bhaskar B, Ortiz de Montellano PR, Poulos TL. Crystal structure of human heme oxygenase-1 in a complex with biliverdin. Biochemistry. 2004 Apr 6;43(13):3793-801. PMID:15049686 doi:10.1021/bi035451l

1. ↑ 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