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Siderocalin

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== Structural highlights ==
== Structural highlights ==
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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>.
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Scn-NGAL interacts with the 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>.
</StructureSection>
</StructureSection>

Revision as of 10:47, 25 December 2016

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

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3D structures of siderocalin

Updated on 25-December-2016

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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

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