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- W2041745886 abstract "Pb2+ is known to displace physiologically-relevant metal ions in proteins. To investigate potential relationships between Pb2+/protein complexes and toxicity, data from the protein data bank were analyzed to compare structural properties of Pb2+- and Ca2+-binding sites. Results of this analysis reveal that the majority of Pb2+ sites (77.1%) involve 2–5 binding ligands, compared with 6 ± 2 for non-EF-Hand and 7 ± 1 for EF-Hand Ca2+-binding sites. The mean net negative charge by site (1.7) fell between values noted for non-EF-Hand (1 ± 1) and EF-Hand (3 ± 1). Oxygen is the dominant ligand for both Pb2+ and Ca2+, but Pb2+ binds predominantly with sidechain Glu (38.4%), which is less prevalent in both non-EF-Hand (10.4%) and EF-Hand (26.6%) Ca2+-binding sites. A comparison of binding geometries where Pb2+ has replaced Ca2+ in calmodulin (CaM) and Zn2+ in 5-aminolaevulinic acid dehydratase (ALAD) revealed protein structural changes that appear to be unrelated to ionic displacement. Structural changes observed with CaM may be related to opportunistic binding of Pb2+ in regions of high electrostatic charge, whereas ALAD may bind multiple Pb2+ ions in the active site. These results suggest that Pb2+ adapts to structurally-diverse binding geometries and that opportunistic binding may play an active role in molecular metal toxicity." @default.
- W2041745886 created "2016-06-24" @default.
- W2041745886 creator A5025670628 @default.
- W2041745886 creator A5062706695 @default.
- W2041745886 date "2008-10-01" @default.
- W2041745886 modified "2023-10-14" @default.
- W2041745886 title "Structural differences between Pb2+- and Ca2+-binding sites in proteins: Implications with respect to toxicity" @default.
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- W2041745886 doi "https://doi.org/10.1016/j.jinorgbio.2008.06.014" @default.
- W2041745886 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2567809" @default.
- W2041745886 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18684507" @default.
- W2041745886 hasPublicationYear "2008" @default.
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