1l6m: Difference between revisions
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'''Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition''' | {{Structure | ||
|PDB= 1l6m |SIZE=350|CAPTION= <scene name='initialview01'>1l6m</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=DBH:2,3-DIHYDROXY-BENZOIC+ACID'>DBH</scene> and <scene name='pdbligand=DBS:2-(2,3-DIHYDROXY-BENZOYLAMINO)-3-HYDROXY-PROPIONIC ACID'>DBS</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Neutrophil Gelatinase-associated Lipocalin is a Novel Bacteriostatic Agent that Interferes with Siderophore-mediated Iron Acquisition''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1L6M is a [ | 1L6M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6M OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12453412 12453412] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: siderophore]] | [[Category: siderophore]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:27:05 2008'' | ||
Revision as of 13:27, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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