2kt4

Lipocalin Q83 is a Siderocalin

spinqualitylabelsall models 2kt4, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kt4 is a 1 chain structure with sequence from Cotja. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EB4, GA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [EXFAB_COTJA] Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Siderocalins are atypical lipocalins able to capture siderophores with high affinity. They contribute to the innate immune response by interfering with bacterial siderophore-mediated iron uptake but are also involved in numerous physiological processes such as inflammation, iron delivery, tissue differentiation, and cancer progression. The Q83 lipocalin was originally identified based on its overexpression in quail embryo fibroblasts transformed by the v-myc oncogene. We show here that Q83 is a siderocalin, binding the siderophore enterobactin with an affinity and mode of binding nearly identical to that of neutrophil gelatinase-associated lipocalin (NGAL), the prototypical siderocalin. This strengthens the role of siderocalins in cancer progression and inflammation. In addition, we also present the solution structure of Q83 in complex with intact enterobactin and a detailed analysis of the Q83 binding mode, including mutagenesis of the critical residues involved in enterobactin binding. These data provide a first insight into the molecular details of siderophore binding and delineate the common molecular properties defining the siderocalin protein family. The v-myc-induced Q83 lipocalin is a siderocalin.,Coudevylle N, Geist L, Hotzinger M, Hartl M, Kontaxis G, Bister K, Konrat R J Biol Chem. 2010 Dec 31;285(53):41646-52. Epub 2010 Sep 8. PMID:20826777 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Siderocalin

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