Neutrophil gelatinase-associated lipocalin

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spinqualitylabelsall models Structure of human neutrophil gelatinase-associated lipocalin complex with Fe+3 ion and carboxymycobactin (PDB code 1x71). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 Structural highlights Function Neutrophil gelatinase-associated lipocalin (NGAL) or lipocalin-2 is involved in innate immunity by sequestering bacterial iron and thus preventing bacterial growth[1]. Lipocalin-1 (Lcn1) or Tear lipocalin is a major protein in tears which binds diverse set of lipophilic molecules [2]. Relevance NGAL is secreted in high levels into the blood following acute kidney injury and thus can be used as a biomarker for it[3]. Lcn1 functions in tears includes their viscosity and it serves as biomarker for dry eyes. Structural highlights NGAL binds siderophores like carboxymycobactin or enterobactin with cation-π interactions and an Fe+3 ion[4]. Structural highlights

3D structures of neutrophil gelatinase-associated lipocalin

Updated on 11-May-2016

References

1. ↑ Friedl A, Stoesz SP, Buckley P, Gould MN. Neutrophil gelatinase-associated lipocalin in normal and neoplastic human tissues. Cell type-specific pattern of expression. Histochem J. 1999 Jul;31(7):433-41. PMID:10475571
2. ↑ Dartt DA. Tear lipocalin: structure and function. Ocul Surf. 2011 Jul;9(3):126-38. PMID:21791187
3. ↑ Viau A, El Karoui K, Laouari D, Burtin M, Nguyen C, Mori K, Pillebout E, Berger T, Mak TW, Knebelmann B, Friedlander G, Barasch J, Terzi F. Lipocalin 2 is essential for chronic kidney disease progression in mice and humans. J Clin Invest. 2010 Nov;120(11):4065-76. doi: 10.1172/JCI42004. PMID:20921623 doi:http://dx.doi.org/10.1172/JCI42004
4. ↑ Holmes MA, Paulsene W, Jide X, Ratledge C, Strong RK. Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration. Structure. 2005 Jan;13(1):29-41. PMID:15642259 doi:10.1016/j.str.2004.10.009