Siderocalin
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | <StructureSection load='1x89' size='340' side='right' caption=' | + | <StructureSection load='1x89' size='340' side='right' caption='Human siderocalin complex with the siderophore carboxymycobactin (PDB code [[1x89]])' 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>. | ||
Line 5: | Line 5: | ||
== Relevance == | == 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<ref>PMID:22728330</ref>. | 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<ref>PMID:22728330</ref>. | ||
+ | |||
+ | == Structural highlights == | ||
+ | Scn-NGAL interacts with the siderophore carboxymycobactin where the latter is centered in the protein calyx making multiple interactions including cation-π bonds involving several lysines and arginine<ref>PMID:15642259</ref>. | ||
</StructureSection> | </StructureSection> |
Revision as of 09:43, 25 December 2016
|
3D structures of siderocalin
Updated on 25-December-2016
>
References
- ↑ 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