3u03
From Proteopedia
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==The structure of Human Siderocalin bound to the bacterial siderophore pyochelin== | ==The structure of Human Siderocalin bound to the bacterial siderophore pyochelin== | ||
<StructureSection load='3u03' size='340' side='right' caption='[[3u03]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3u03' size='340' side='right' caption='[[3u03]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3u03]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3u03]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U03 FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=488:(2R,4R)-2-[(4R)-2-(2-HYDROXYPHENYL)-4,5-DIHYDRO-1,3-THIAZOL-4-YL]-3-METHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>488</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=488:(2R,4R)-2-[(4R)-2-(2-HYDROXYPHENYL)-4,5-DIHYDRO-1,3-THIAZOL-4-YL]-3-METHYL-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>488</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LCN2, HNL, NGAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LCN2, HNL, NGAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u03 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u03 RCSB], [http://www.ebi.ac.uk/pdbsum/3u03 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u03 OCA], [http://pdbe.org/3u03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u03 RCSB], [http://www.ebi.ac.uk/pdbsum/3u03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u03 ProSAT]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NGAL_HUMAN NGAL_HUMAN]] Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis. Involved in innate immunity, possibly by sequestrating iron, leading to limit bacterial growth.<ref>PMID:12453413</ref> | ||
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| + | ==See Also== | ||
| + | *[[Neutrophil gelatinase-associated lipocalin|Neutrophil gelatinase-associated lipocalin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
[[Category: Antimicrobial protein]] | [[Category: Antimicrobial protein]] | ||
[[Category: Beta-barrel]] | [[Category: Beta-barrel]] | ||
[[Category: Siderocalin]] | [[Category: Siderocalin]] | ||
[[Category: Siderophore]] | [[Category: Siderophore]] | ||
| - | [[Category: Ssgcid seattle structural genomics center for infectious disease]] | ||
Current revision
The structure of Human Siderocalin bound to the bacterial siderophore pyochelin
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