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| [[Image:1l6m.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1l6m.png|left|200px]] |
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| {{STRUCTURE_1l6m| PDB=1l6m | SCENE= }} | | {{STRUCTURE_1l6m| PDB=1l6m | SCENE= }} |
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| '''Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition'''
| | ===Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12453412}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12453412 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12453412}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lipocalin]] | | [[Category: Lipocalin]] |
| [[Category: Siderophore]] | | [[Category: Siderophore]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:35:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:48:52 2008'' |