The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: Mapping of human 14-3-3 zeta homodimer interface

0388476 - MBÚ 2013 RIV US eng J - Článek v odborném periodiku
Haladová, Kateřina - Mrázek, Hynek - Ječmen, Tomáš - Halada, Petr - Man, Petr - Novák, Petr - Chmelík, Josef - Obšil, Tomáš - Šulc, Miroslav
The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: Mapping of human 14-3-3 zeta homodimer interface.
Journal of Structural Biology. Roč. 179, č. 1 (2012), s. 10-17. ISSN 1047-8477. E-ISSN 1095-8657
Grant CEP: GA ČR GAP207/12/0627; GA ČR GD305/09/H008
Institucionální podpora: RVO:61388971 ; RVO:67985823
Klíčová slova: Protein-protein interaction * 14-3-3 Homodimer * Chemical cross-linking
Kód oboru RIV: CE - Biochemie
Impakt faktor: 3.361, rok: 2012

Hydrogen/deuterium (H/D) exchange or chemical cross-linking by soluble carbodiimide (EDC) was employed in combination with high-resolution mass spectrometry (MS) to extend our knowledge about contact surface regions involved in the well-characterized model of interaction between two molecules of human 14-3-3 zeta regulatory protein. The H/D exchange experiment provided low resolution mapping of interaction in the homodimeric 14-3-3 zeta complex. A lower level of deuteration, suggesting structural protection, of two sequential segments has been demonstrated for dimeric 14-3-3 zeta wild type relative to the monomeric mutant 14-3-3 zeta S58D. The N-terminal sequence (the first 27 residues) from one subunit interacts with region alpha C' and alpha D'-helices (residues 45-98) of the other molecule across the dimer interface
Trvalý link: http://hdl.handle.net/11104/0217376