Siderocalin

From Proteopedia

Revision as of 09:24, 3 November 2020

spinqualitylabelsall models Human siderocalin complex with the siderophore carboxymycobactin (PDB code 1x89) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Siderocalin (Scn) or neutrophil gelatinase-associated lipocalin binds ferric siderophores in order to intercept delivery of iron to bacteria which require it thus impeding their virulence[1]. Relevance Scn-NGAL levels are markedly upregulated by tissue damage. Scn-NGAL is derived from damaged kidneys. The presence of Scn-NGAL in serum or urine anticipates a severe course for the patient including the need for dialysis and the possibility of death[2]. Structural highlights Scn-NGAL interacts with the making [3]. Water molecules are shown as red spheres. .

3D structures of siderocalin

Updated on 03-November-2020

References

1. ↑ Hoette TM, Abergel RJ, Xu J, Strong RK, Raymond KN. The role of electrostatics in siderophore recognition by the immunoprotein Siderocalin. J Am Chem Soc. 2008 Dec 24;130(51):17584-92. doi: 10.1021/ja8074665. PMID:19053425 doi:http://dx.doi.org/10.1021/ja8074665
2. ↑ Paragas N, Qiu A, Hollmen M, Nickolas TL, Devarajan P, Barasch J. NGAL-Siderocalin in kidney disease. Biochim Biophys Acta. 2012 Sep;1823(9):1451-8. doi: 10.1016/j.bbamcr.2012.06.014., Epub 2012 Jun 19. PMID:22728330 doi:http://dx.doi.org/10.1016/j.bbamcr.2012.06.014
3. ↑ Holmes MA, Paulsene W, Jide X, Ratledge C, Strong RK. Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration. Structure. 2005 Jan;13(1):29-41. PMID:15642259 doi:10.1016/j.str.2004.10.009