1l6m
Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition
|
OverviewOverview
First identified as a neutrophil granule component, neutrophil, gelatinase-associated lipocalin (NGAL; also called human neutrophil, lipocalin, 24p3, uterocalin, or neu-related lipocalin) is a member of the, lipocalin family of binding proteins. Putative NGAL ligands, including, neutrophil chemotactic agents such as N-formylated tripeptides, have all, been refuted by recent biochemical and structural results. NGAL has, subsequently been implicated in diverse cellular processes, but without a, characterized ligand, the molecular basis of these functions remained, mysterious. Here we report that NGAL tightly binds bacterial, catecholate-type ferric siderophores through a cyclically permuted, hybrid, electrostatic/cation-pi interaction and is a potent bacteriostatic agent, in iron-limiting conditions. We therefore propose that NGAL participates, in the antibacterial iron depletion strategy of the innate immune system.
About this StructureAbout this Structure
1L6M is a Single protein structure of sequence from Homo sapiens with FE, SO4, DBH and DBS as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition., Goetz DH, Holmes MA, Borregaard N, Bluhm ME, Raymond KN, Strong RK, Mol Cell. 2002 Nov;10(5):1033-43. PMID:12453412
Page seeded by OCA on Mon Nov 12 17:57:19 2007