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Siderocalin
From Proteopedia
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<StructureSection load='' size='350' side='right' caption='Human siderocalin complex with the siderophore carboxymycobactin (PDB code [[1x89]])' scene='48/488406/Cv/1' > | <StructureSection load='' size='350' side='right' caption='Human siderocalin complex with the siderophore carboxymycobactin (PDB code [[1x89]])' scene='48/488406/Cv/1' > | ||
| + | __TOC__ | ||
== Function == | == 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<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>. | ||
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Scn-NGAL interacts with the <scene name='48/488406/Cv/4'>siderophore carboxymycobactin where the latter is centered in the protein calyx</scene> making <scene name='48/488406/Cv/5'>multiple interactions including cation-π bonds involving several lysines and arginine</scene><ref>PMID:15642259</ref>. Water molecules are shown as red spheres. <scene name='48/488406/Cv/6'>Fe coordination site</scene>. | Scn-NGAL interacts with the <scene name='48/488406/Cv/4'>siderophore carboxymycobactin where the latter is centered in the protein calyx</scene> making <scene name='48/488406/Cv/5'>multiple interactions including cation-π bonds involving several lysines and arginine</scene><ref>PMID:15642259</ref>. Water molecules are shown as red spheres. <scene name='48/488406/Cv/6'>Fe coordination site</scene>. | ||
| - | </StructureSection> | ||
==3D structures of siderocalin== | ==3D structures of siderocalin== | ||
| + | [[Siderocalin 3D structures]] | ||
| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *Siderocalin or lipocalin-2 | ||
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| - | **[[5jr8]], [[3bx8]], [[5khp]], [[5kid]], [[5kic]], [[5mhh]], [[6gqz]], [[1qqs]] – hScn NGAL - human<br /> | ||
| - | **[[1l6m]], [[3dtq]], [[4iaw]], [[4iax]], [[6qmu]] – hScn NGAL (mutant)<br /> | ||
| - | **[[3s26]] – mScn NGAL - mouse<br /> | ||
| - | **[[2k23]] – Scn NGAL – rat - NMR<br /> | ||
| - | **[[2kt4]] – qScn Q83 – quail<br /> | ||
| - | |||
| - | *Siderocalin complex | ||
| - | |||
| - | **[[4mvi]], [[4mvk]], [[4mvl]] – hScn NGAL (mutant) + β-amyloid protein 40 peptide<br /> | ||
| - | **[[3bx7]] – hScn NGAL + CTLA-4<br /> | ||
| - | **[[3tzs]] – hScn NGAL (mutant) + phenylurea<br /> | ||
| - | **[[4zfx]], [[4zhc]], [[4zhd]], [[4zhf]], [[4zhg]], [[4zhh]], [[4qae]], [[4k19]], [[4aiw]], [[4aix]], [[6o5d]], [[3u0d]], [[3k3l]], [[3dsz]], [[1x89]], [[1x8u]], [[1x71]] – hScn NGAL + siderophore<br /> | ||
| - | **[[3tf6]], [[3t1d]], [[3i0a]], [[3hwd]] – hScn NGAL (mutant) + siderophore<br /> | ||
| - | **[[3pec]], [[3ped]] – hScn NGAL + siderophore + Fe<br /> | ||
| - | **[[3hwe]], [[3hwf]], [[3hwg]], [[3cmp]], [[3by0]], [[3cbc]] – hScn NGAL (mutant) + siderophore + Fe<br /> | ||
| - | **[[3fw4]], [[3fw5]] – hScn NGAL (mutant) + catechol + Fe<br /> | ||
| - | **[[4gh7]], [[5n48]], [[5n47]] – hScn NGAL + fibronectin<br /> | ||
| - | **[[5nkn]] – hScn NGAL + conchicine<br /> | ||
| - | **[[6gr0]] – hScn NGAL + petrobactin<br /> | ||
| - | **[[3u9p]] – mScn NGAL + Fab <br /> | ||
| - | **[[2lbv]] – qScn Q83 + enterobactin – NMR<br /> | ||
| - | **[[3sao]] – cScn + myristoyl lysophosphatidic acid - chicken<br /> | ||
| - | > | ||
| - | |||
| - | }} | ||
==References== | ==References== | ||
| + | </StructureSection> | ||
<references /> | <references /> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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- ↑ 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
