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Solution structure of the ASHH2 CW domain with the N-terminal histone H3 tail mimicking peptide monomethylated on lysine 4
分子名称:	ALA-ARG-THR-MLZ-GLN-THR-ALA-ARG-TYR, Histone-lysine N-methyltransferase ASHH2, ZINC ION
著者	Dobrovolska, O, Madeleine, N, Teigen, K, Halskau, O, Bril'kov, M.
登録日	2019-03-08
公開日	2019-12-04
最終更新日	2023-06-14
実験手法	SOLUTION NMR
主引用文献	The Arabidopsis (ASHH2) CW domain binds monomethylated K4 of the histone H3 tail through conformational selection. Febs J., 287, 2020

The polyserine tract of Nasonia vitripennis Vg residues 351-385
分子名称:	Vitellogenin
著者	Havukainen, H, Halskau Jr, O.
登録日	2011-08-29
公開日	2012-07-11
最終更新日	2022-03-09
実験手法	SOLUTION NMR
主引用文献	A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. J Exp Biol, 215, 2012

NMR Structure of the Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392
分子名称:	Vitellogenin
著者	Havukainen, H, Halskau Jr, O.
登録日	2011-08-29
公開日	2012-08-22
実験手法	SOLUTION NMR
主引用文献	A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. J Exp Biol, 215, 2012

14-3-3gamma complexed with the N-terminal sequence of tyrosine hydroxylase (residues 1-43)
分子名称:	14-3-3 protein gamma, N-terminal motif of tyrosine hydroxylase
著者	Mileni, M, Martinez, A, Stevens, R.C.
登録日	2013-02-11
公開日	2013-10-02
最終更新日	2023-09-20
実験手法	X-RAY DIFFRACTION (3.08 Å)
主引用文献	The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes. J.Mol.Biol., 426, 2014