Siderocalin: Difference between revisions

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<StructureSection load='4zfx' size='340' side='right' caption='Yeast Holliday junction resolvase dimer complex with sulfate, [[1kcf]]' scene='' >
<StructureSection load='1x89' size='340' side='right' caption='Yeast Holliday junction resolvase dimer complex with sulfate, [[1kcf]]' scene='' >
== Function ==
== 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) binds ferric siderophores in order to intercept delivery of iron to bacteria which require it thus  impeding their virulence<ref>PMID:19053425</ref>.


== Relevance ==
== Relevance ==

Revision as of 12:38, 25 December 2016

Function

Siderocalin (Scn) 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].


Yeast Holliday junction resolvase dimer complex with sulfate, 1kcf

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3D structures of siderocalin3D structures of siderocalin

Updated on 25-December-2016

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ReferencesReferences

  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

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Alexander Berchansky, Michal Harel, Joel L. Sussman