1l6m: Difference between revisions

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==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bluhm, M.E.]]
[[Category: Bluhm, M E.]]
[[Category: Borregaard, N.]]
[[Category: Borregaard, N.]]
[[Category: Goetz, D.H.]]
[[Category: Goetz, D H.]]
[[Category: Raymond, K.N.]]
[[Category: Raymond, K N.]]
[[Category: Strong, R.K.]]
[[Category: Strong, R K.]]
[[Category: DBH]]
[[Category: DBH]]
[[Category: DBS]]
[[Category: DBS]]
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[[Category: siderophore]]
[[Category: siderophore]]


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Revision as of 14:41, 21 February 2008

File:1l6m.jpg


1l6m, resolution 2.40Å

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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 , , and 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

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