IQUIFIB 02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
artículos
Título:
1H, 13C and 15N resonance assignments of parvulin 17
Autor/es:
YI-JAN LIN; ANDREAS SCHMIDT; NOELIA INÉS BURGARDT; ALEXANDRA THIELE; GUNTER FISCHER; MATTHIAS WEIWAD; CHRISTIAN LÜCKE
Revista:
BIOMOLECULAR NMR ASSIGNMENTS
Editorial:
SPRINGER
Referencias:
Lugar: Berlin; Año: 2013 vol. 7 p. 325 - 329
ISSN:
1874-2718
Resumen:
A 25-residue elongation at the N-terminus endows parvulin 17 (Par17) with altered functional properties compared to parvulin 14 (Par14), such as an enhanced influence on microtubule assembly. Therefore the three-dimensional structure of this N-terminal elongation is of particular interest. Here, we report the nearly complete (1)H, (13)C and (15)N chemical shift assignments of Par17. Subsequent chemical shift index analysis indicated that Par17 features a parvulin-type PPIase domain at the C-terminus, analogous to Par14, and an unstructured N-terminus encompassing the first 60 residues. Hence the N-terminus of Par17 apparently adopts a functionally-relevant structure only in presence of the respective interaction partner(s).
