期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 291, 期 6, 页码 2917-2930出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M115.685644
关键词
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资金
- European Union from the European Regional Development Fund under the Operational Programme Innovative Economy
- Austrian Science Fund (FWF) [P 27347, P 24761, Y 372] Funding Source: researchfish
- Austrian Science Fund (FWF) [P27347, P24761] Funding Source: Austrian Science Fund (FWF)
The neutrophil gelatinase-associated lipocalin (NGAL, also known as LCN2) and its cellular receptor (LCN2-R, SLC22A17) are involved in many physiological and pathological processes such as cell differentiation, apoptosis, and inflammation. These pleiotropic functions mainly rely on NGAL's siderophore-mediated iron transport properties. However, the molecular determinants underlying the interaction between NGAL and its cellular receptor remain largely unknown. Here, using solution-state biomolecular NMR in conjunction with other biophysical methods, we show that the N-terminal domain of LCN2-R is a soluble extracellular domain that is intrinsically disordered and interacts with NGAL preferentially in its apo state to form a fuzzy complex. The relatively weak affinity (approximate to 10 mu M) between human LCN2-R-NTD and apo NGAL suggests that the N terminus on its own cannot account for the internalization of NGAL by LCN2-R. However, human LCN2-R-NTD could be involved in the fine-tuning of the interaction between NGAL and its cellular receptor or in a biochemical mechanism allowing the receptor to discriminate between apo- and holo-NGAL.
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