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| == Structural highlights == | | == Structural highlights == |
| Scn-NGAL interacts with the <scene name='48/488406/Cv/3'>siderophore carboxymycobactin where the latter is centered in the protein calyx</scene>siderophore carboxymycobactin where the latter is centered in the protein calyx making <scene name='48/488406/Cv/2'>multiple interactions including cation-π bonds involving several lysines and arginine</scene><ref>PMID:15642259</ref>. | | Scn-NGAL interacts with the <scene name='48/488406/Cv/3'>siderophore carboxymycobactin where the latter is centered in the protein calyx</scene> making <scene name='48/488406/Cv/2'>multiple interactions including cation-π bonds involving several lysines and arginine</scene><ref>PMID:15642259</ref>. |
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| </StructureSection> | | </StructureSection> |
Revision as of 10:51, 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].
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[3].
- ↑ 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:https://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:https://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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3D structures of siderocalin
Updated on 25-December-2016
{"openlevels":0}
- Siderocalin or lipocalin-2
- Siderocalin complex
- 4mvi, 4mvk, 4mvl – hScn NGAL (mutant) + beta amyloid protein 40 peptide
- 3bx7 – hScn NGAL + CTLA-4
- 3tzs – hScn NGAL (mutant) + phenylurea
- 4zfx, 4zhc, 4zhd, 4zhf, 4zhg, 4zhh, 4qae, 4k19, 4aiw, 4aix, 3u03, 3u0d, 3k3l, 3dsz, 1x89, 1x8u, 1x71 – hScn NGAL + siderophore
- 3tf6, 3t1d, 3i0a, 3hwd – hScn NGAL (mutant) + siderophore
- 3pec, 3ped – hScn NGAL + siderophore + Fe
- 3hwe, 3hwf, 3hwg, 3cmp, 3by0, 3cbc – hScn NGAL (mutant) + siderophore + Fe
- 3fw4, 3fw5 – hScn NGAL (mutant) + catechol + Fe
- 4gh7 – hScn NGAL + fibronectin
- 3u9p – mScn NGAL + Fab
- 2lbv – qScn Q83 + enterobactin – NMR
- 3sao – cScn + myristoyl lysophosphatidic acid - chicken
>
References
