1l6m: Difference between revisions
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|PDB= 1l6m |SIZE=350|CAPTION= <scene name='initialview01'>1l6m</scene>, resolution 2.40Å | |PDB= 1l6m |SIZE=350|CAPTION= <scene name='initialview01'>1l6m</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=DBH:2,3-DIHYDROXY-BENZOIC+ACID'>DBH</scene>, <scene name='pdbligand=DBS:2-(2,3-DIHYDROXY-BENZOYLAMINO)-3-HYDROXY-PROPIONIC+ACID'>DBS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1dfv|1dfv]], [[1qqs|1qqs]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6m OCA], [http://www.ebi.ac.uk/pdbsum/1l6m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l6m RCSB]</span> | |||
}} | }} | ||
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[[Category: Raymond, K N.]] | [[Category: Raymond, K N.]] | ||
[[Category: Strong, R K.]] | [[Category: Strong, R K.]] | ||
[[Category: lipocalin]] | [[Category: lipocalin]] | ||
[[Category: siderophore]] | [[Category: siderophore]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:58:49 2008'' | ||
Revision as of 21:58, 30 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | , , , | ||||||
| Related: | 1dfv, 1qqs
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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