1x89: Difference between revisions
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|PDB= 1x89 |SIZE=350|CAPTION= <scene name='initialview01'>1x89</scene>, resolution 2.1Å | |PDB= 1x89 |SIZE=350|CAPTION= <scene name='initialview01'>1x89</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CM1:CARBOXYMYCOBACTIN S'>CM1</scene> | |LIGAND= <scene name='pdbligand=CM1:CARBOXYMYCOBACTIN+S'>CM1</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= LCN2, NGAL, HNL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= LCN2, NGAL, HNL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1x71|1X71]], [[1x8u|1X8U]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x89 OCA], [http://www.ebi.ac.uk/pdbsum/1x89 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x89 RCSB]</span> | |||
}} | }} | ||
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[[Category: Ratledge, C.]] | [[Category: Ratledge, C.]] | ||
[[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 Mon Mar 31 00:46:03 2008'' | ||
Revision as of 00:46, 31 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | |||||||
| Gene: | LCN2, NGAL, HNL (Homo sapiens) | ||||||
| Related: | 1X71, 1X8U
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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