Backbone chemical shift and secondary structure assignments for mouse siderocalin.

Autor: Moeller J; Institute for Drug Discovery, Leipzig University Medical School, 04103, Leipzig, Germany.; Center for Scalable Data Analytics and Artificial Intelligence (ScaDS.AI) Dresden/Leipzig, Leipzig University, Leipzig, Germany., Bozhanova NG; Center for Structural Biology, Vanderbilt University, Nashville, TN, 37232, USA.; Department of Chemistry, Vanderbilt University, Nashville, TN, 37232, USA., Voehler M; Center for Structural Biology, Vanderbilt University, Nashville, TN, 37232, USA.; Department of Chemistry, Vanderbilt University, Nashville, TN, 37232, USA., Meiler J; Institute for Drug Discovery, Leipzig University Medical School, 04103, Leipzig, Germany.; Center for Structural Biology, Vanderbilt University, Nashville, TN, 37232, USA.; Department of Chemistry, Vanderbilt University, Nashville, TN, 37232, USA., Schoeder CT; Institute for Drug Discovery, Leipzig University Medical School, 04103, Leipzig, Germany. clara.schoeder@medizin.uni-leipzig.de.; Center for Scalable Data Analytics and Artificial Intelligence (ScaDS.AI) Dresden/Leipzig, Leipzig University, Leipzig, Germany. clara.schoeder@medizin.uni-leipzig.de.
Jazyk: angličtina
Zdroj: Biomolecular NMR assignments [Biomol NMR Assign] 2024 Jun; Vol. 18 (1), pp. 79-84. Date of Electronic Publication: 2024 Apr 02.
DOI: 10.1007/s12104-024-10171-9
Abstrakt: The lipocalin protein family is a structurally conserved group of proteins with a variety of biological functions defined by their ability to bind small molecule ligands and interact with partner proteins. One member of this family is siderocalin, a protein found in mammals. Its role is discussed in inflammatory processes, iron trafficking, protection against bacterial infections and oxidative stress, cell migration, induction of apoptosis, and cancer. Though it seems to be involved in numerous essential pathways, the exact mechanisms are often not fully understood. The NMR backbone assignments for the human siderocalin and its rat ortholog have been published before. In this work we describe the backbone NMR assignments of siderocalin for another important model organism, the mouse - data that might become important for structure-based drug discovery. Secondary structure elements were predicted based on the assigned backbone chemical shifts using TALOS-N and CSI 3.0, revealing a high content of beta strands and one prominent alpha helical region. Our findings correlate well with the known crystal structure and the overall conserved fold of the lipocalin family.
(© 2024. The Author(s).)
Databáze: MEDLINE
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