2kzd | pdb_00002kzd
From Proteopedia
Structure of a (3+1) G-quadruplex formed by hTERT promoter sequence
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Structural highlights
Publication Abstract from PubMedThe catalytic subunit of human telomerase, hTERT, actively elongates the 3' end of the telomere in most cancer cells. The hTERT promoter, which contains many guanine-rich stretches on the same DNA strand, exhibits an exceptional potential for G-quadruplex formation. Here we show that one particular G-rich sequence in this region coexists in two G-quadruplex conformations in potassium solution: a (3 + 1) and a parallel-stranded G-quadruplexes. We present the NMR solution structures of both conformations, each comprising several robust structural elements, among which include the (3 + 1) and all-parallel G-tetrad cores, single-residue double-chain-reversal loops, and a capping A.T base pair. A combination of NMR and CD techniques, complemented with sequence modifications and variations of experimental condition, allowed us to better understand the coexistence of the two G-quadruplex conformations in equilibrium and how different structural elements conspire to favor a particular form. Coexistence of two distinct G-quadruplex conformations in the hTERT promoter.,Lim KW, Lacroix L, Yue DJ, Lim JK, Lim JM, Phan AT J Am Chem Soc. 2010 Sep 8;132(35):12331-42. PMID:20704263[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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