7d32
From Proteopedia
The TBA-Pb2+ complex in P41212 space group
Structural highlights
Publication Abstract from PubMedOwing to its great threat to human health and environment, Pb(2+) pollution has been recognized as a major public problem by the World Health Organization (WHO). Many DNA aptamers have been utilized in the development of Pb(2+)-detection sensors, but the underlying mechanisms remain elusive. Here, we report three Pb(2+)-complexed structures of the thrombin binding aptamer (TBA). These high-resolution crystal structures showed that TBA forms intramolecular G-quadruplex and Pb(2+) is bound by the two G-tetrads in the center. Compared to K(+)-stabilized G-quadruplexes, the coordinating distance between Pb(2+) and the G-tetrads are much shorter. The T3T4 and T12T13 linkers play important roles in dimerization and crystallization of TBA, but they are changeable for Pb(2+)-binding. In combination with mutagenesis and CD spectra, the G8C mutant structure unraveled that the T7G8T9 linker of TBA is also variable. In addition to expansion of the Pb(2+)-binding aptamer sequences, our study also set up one great example for quick and rational development of other aptamers with similar or optimized binding activity. Structure-guided development of Pb(2+)-binding DNA aptamers.,Liu H, Gao Y, Mathivanan J, Shen F, Chen X, Li Y, Shao Z, Zhang Y, Shao Q, Sheng J, Gan J Sci Rep. 2022 Jan 10;12(1):460. doi: 10.1038/s41598-021-04243-2. PMID:35013452[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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