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Solution structure of the ASHH2 CW domain with the N-terminal histone H3 tail mimicking peptide monomethylated on lysine 4
Descriptor:	ALA-ARG-THR-MLZ-GLN-THR-ALA-ARG-TYR, Histone-lysine N-methyltransferase ASHH2, ZINC ION
Authors:	Dobrovolska, O, Madeleine, N, Teigen, K, Halskau, O, Bril'kov, M.
Deposit date:	2019-03-08
Release date:	2019-12-04
Last modified:	2023-06-14
Method:	SOLUTION NMR
Cite:	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
Descriptor:	Vitellogenin
Authors:	Havukainen, H, Halskau Jr, O.
Deposit date:	2011-08-29
Release date:	2012-07-11
Last modified:	2024-10-30
Method:	SOLUTION NMR
Cite:	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
Descriptor:	Vitellogenin
Authors:	Havukainen, H, Halskau Jr, O.
Deposit date:	2011-08-29
Release date:	2012-08-22
Method:	SOLUTION NMR
Cite:	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)
Descriptor:	14-3-3 protein gamma, N-terminal motif of tyrosine hydroxylase
Authors:	Mileni, M, Martinez, A, Stevens, R.C.
Deposit date:	2013-02-11
Release date:	2013-10-02
Last modified:	2023-09-20
Method:	X-RAY DIFFRACTION (3.08 Å)
Cite:	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