Siderocalin: Difference between revisions

Revision as of 01:49, 4 October 2017

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].

Human siderocalin complex with the siderophore carboxymycobactin (PDB code 1x89)

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3D structures of siderocalin3D structures of siderocalin

Updated on 04-October-2017

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ReferencesReferences

↑ 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
↑ 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
↑ 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

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Alexander Berchansky, Michal Harel, Joel L. Sussman

[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

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@@ Line 1: / Line 1: @@
 <StructureSection load='1x89' size='450' side='right' caption='Human siderocalin complex with the siderophore carboxymycobactin (PDB code [[1x89]])' scene='48/488406/Cv/1' >
 == Function ==
-'''Siderocalin''' (Scn) binds ferric siderophores in order to intercept delivery of iron to bacteria which require it thus  impeding their virulence<ref>PMID:19053425</ref>.
+'''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<ref>PMID:19053425</ref>.
 == Relevance ==
@@ Line 16: / Line 16: @@
 *Siderocalin or lipocalin-2
-**[[5jr8]], [[3bx8]] – hScn NGAL - human<br />
+**[[5jr8]], [[3bx8]], [[5khp]], [[5kid]], [[5kic]] – hScn NGAL - human<br />
 **[[3s26]] – mScn NGAL - mouse<br />
 **[[2kt4]] – qScn Q83 – quail<br />
@@ Line 22: / Line 22: @@
 *Siderocalin complex
-**[[4mvi]], [[4mvk]], [[4mvl]] – hScn NGAL (mutant) + beta amyloid protein 40 peptide<br />
+**[[4mvi]], [[4mvk]], [[4mvl]] – hScn NGAL (mutant) + β-amyloid protein 40 peptide<br />
 **[[3bx7]] – hScn NGAL + CTLA-4<br />
 **[[3tzs]] – hScn NGAL (mutant) + phenylurea<br />