Birch pollen profilin: structural organization and interaction with poly‐(l‐proline) peptides as revealed by NMR

FEBS Letters

Federau, Torsten²  Domke, Tobias²  Schlüter, Kathrin¹  Schomburg, Dietmar²  Giehl, Klaudia¹  Valenta, Rudolf³  Jockusch, Brigitte M.¹ 

[1] Cell Biology, Zoological Institute, Technische Universität Braunschweig, D-38092 Braunschweig, Germany;Molecular Structure Research, Gesellschaft für Biotechnologische Forschung, Mascheroder Weg 1, D-38124 Braunschweig, Germany;Institute of General and Experimental Pathology, University of Vienna, Währinger Gürtel 18-20, A-1090 Vienna, Austria

关键词: Birch profilin;    Nuclear magnetic resonance;    Poly-(l-proline) motif;    Microfilament;    Signal transduction;   

DOI  :  10.1016/S0014-5793(97)00719-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The secondary structure of birch pollen profilin, a potent human allergen, was elucidated by multidimensional nuclear magnetic resonance (NMR), as a prerequisite to study the interaction of this profilin with ligands for its poly-(l-proline) (PLP)-binding site. The chemical shifts of the ¹⁵N-labeled backbone amide groups were used to monitor complex formation with various PLP peptides. Titration with deca-l-proline (P₁₀) yielded a K _D of 0.2 mM. P₈ was the shortest PLP to provoke a significant reaction. (GP₅)₃G bound significantly, confirming the interaction between profilins and the protein VASP containing this motif. Birch profilin interacted also with GP₆GP₅, found in the cyclase-associated protein (CAP), a suspected profilin ligand.

【 授权许可】

Unknown