1x89: Difference between revisions
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[[Image:1x89.gif|left|200px]] | [[Image:1x89.gif|left|200px]] | ||
'''Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Carboxymycobactin S''' | {{Structure | ||
|PDB= 1x89 |SIZE=350|CAPTION= <scene name='initialview01'>1x89</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CM1:CARBOXYMYCOBACTIN S'>CM1</scene> | |||
|ACTIVITY= | |||
|GENE= LCN2, NGAL, HNL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Carboxymycobactin S''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1X89 is a [ | 1X89 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=1X89 OCA]. | ||
==Reference== | ==Reference== | ||
Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration., Holmes MA, Paulsene W, Jide X, Ratledge C, Strong RK, Structure. 2005 Jan;13(1):29-41. PMID:[http:// | Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration., Holmes MA, Paulsene W, Jide X, Ratledge C, Strong RK, Structure. 2005 Jan;13(1):29-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15642259 15642259] | ||
[[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 15:06:18 2008'' | ||
Revision as of 16:06, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | |||||||
| Gene: | LCN2, NGAL, HNL (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Carboxymycobactin S
OverviewOverview
Siderocalin, a member of the lipocalin family of binding proteins, is found in neutrophil granules, uterine secretions, and at markedly elevated levels in serum and synovium during bacterial infection; it is also secreted from epithelial cells in response to inflammation or tumorigenesis. Identification of high-affinity ligands, bacterial catecholate-type siderophores (such as enterochelin), suggested a possible function for siderocalin: an antibacterial agent, complementing the general antimicrobial innate immune system iron-depletion strategy, sequestering iron as ferric siderophore complexes. Supporting this hypothesis, siderocalin is a potent bacteriostatic agent in vitro under iron-limiting conditions and, when knocked out, renders mice remarkably susceptible to bacterial infection. Here we show that siderocalin also binds soluble siderophores of mycobacteria, including M. tuberculosis: carboxymycobactins. Siderocalin employs a degenerate recognition mechanism to cross react with these dissimilar types of siderophores, broadening the potential utility of this innate immune defense.
About this StructureAbout this Structure
1X89 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration., Holmes MA, Paulsene W, Jide X, Ratledge C, Strong RK, Structure. 2005 Jan;13(1):29-41. PMID:15642259
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