1x89: Difference between revisions

Revision as of 16:52, 21 February 2008

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 with as ligand. 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

Page seeded by OCA on Thu Feb 21 15:52:03 2008

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OCA

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-[[Image:1x89.gif|left|200px]]<br />
+[[Image:1x89.gif|left|200px]]<br /><applet load="1x89" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1x89" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1x89, resolution 2.1&Aring;" />
 '''Crystal structure of Siderocalin (NGAL, Lipocalin 2) complexed with Carboxymycobactin S'''<br />
 ==Overview==
-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.
+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 Structure==
-X89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CM1 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X89 OCA].
+X89 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CM1:'>CM1</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X89 OCA].
 ==Reference==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Holmes, M.A.]]
+[[Category: Holmes, M A.]]
 [[Category: Jide, X.]]
 [[Category: Paulsene, W.]]
 [[Category: Ratledge, C.]]
-[[Category: Strong, R.K.]]
+[[Category: Strong, R K.]]
 [[Category: CM1]]
 [[Category: lipocalin]]
 [[Category: siderophore]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:02:18 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:03 2008''