FEBS Letters | |
Role of modified glutamic acid in the helical structure of conantokin‐T | |
Lin, C.H2  Hsu, K.S3  Lyu, P.C2  King, D.S1  Chen, C.S2  | |
[1] Howard Hughes Medical Institute, 401 Barker Hall, University of California, Berkeley, CA 94720-3202, USA;Department of Life Sciences, National Tsing Hua University, Hsin-chu 30043, Taiwan;Department of Pharmacology, College of Medicine, National Cheng-Kung University, Tainan 701, Taiwan | |
关键词: Conantokin-T; NMDA receptor; γ-Carboxyglutamic acid; Helix; Circular dichroism; NMR; | |
DOI : 10.1016/S0014-5793(97)00354-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Circular dichroism (CD) and 2-dimensional NMR were used to study the solution conformation of conantokin-T (Con-T), a small peptide toxin found in the venom of fish-hunting cone snails, and its Glu-substituted analog. Con-T lacks disulfide bonds but contains many γ-carboxyglutamic acids (Gla), a post-translationally modified residue. Our results show that Con-T adopts an α-helical conformation in aqueous solution even in the absence of calcium. Glu replacements diminish both helicity and function of Con-T. The helical content of Con-T is higher than most natural helical peptides of this length in aqueous solution. The sequence of this small toxin incorporates several known elements that stabilize α-helical structure in peptides. Gla residues form several salt bridges that stabilize helical conformation of Con-T.
【 授权许可】
Unknown
【 预 览 】
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