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3U9P

Crystal Structure of Murine Siderocalin in Complex with an Fab Fragment

Summary for 3U9P
Entry DOI10.2210/pdb3u9p/pdb
DescriptorNeutrophil gelatinase-associated lipocalin, Monoclonal Fab Fragment Heavy Chain, Monoclonal Fab Fragment Light Chain, ... (4 entities in total)
Functional Keywordsbeta barrel, transport protein, immune system
Biological sourceMus musculus (mouse)
More
Cellular locationSecreted : P11672
Total number of polymer chains6
Total formula weight135461.41
Authors
Correnti, C.,Strong, R.K. (deposition date: 2011-10-19, release date: 2013-05-01, Last modification date: 2024-11-06)
Primary citationCorrenti, C.,Richardson, V.,Sia, A.K.,Bandaranayake, A.D.,Ruiz, M.,Suryo Rahmanto, Y.,Kovacevic, Z.,Clifton, M.C.,Holmes, M.A.,Kaiser, B.K.,Barasch, J.,Raymond, K.N.,Richardson, D.R.,Strong, R.K.
Siderocalin/Lcn2/NGAL/24p3 does not drive apoptosis through gentisic acid mediated iron withdrawal in hematopoietic cell lines.
Plos One, 7:e43696-e43696, 2012
Cited by
PubMed Abstract: Siderocalin (also lipocalin 2, NGAL or 24p3) binds iron as complexes with specific siderophores, which are low molecular weight, ferric ion-specific chelators. In innate immunity, siderocalin slows the growth of infecting bacteria by sequestering bacterial ferric siderophores. Siderocalin also binds simple catechols, which can serve as siderophores in the damaged urinary tract. Siderocalin has also been proposed to alter cellular iron trafficking, for instance, driving apoptosis through iron efflux via BOCT. An endogenous siderophore composed of gentisic acid (2,5-dihydroxybenzoic acid) substituents was proposed to mediate cellular efflux. However, binding studies reported herein contradict the proposal that gentisic acid forms high-affinity ternary complexes with siderocalin and iron, or that gentisic acid can serve as an endogenous siderophore at neutral pH. We also demonstrate that siderocalin does not induce cellular iron efflux or stimulate apoptosis, questioning the role siderocalin plays in modulating iron metabolism.
PubMed: 22928018
DOI: 10.1371/journal.pone.0043696
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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