A leucine‐rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a β‐sheet structure

FEBS Letters

Barna, Jennifer C.J.¹  Packman, Leonard C.¹  Weldon, Michael A.¹  Gay, Nicholas J.¹ 

[1] Department of Biochemistry, University of Cambridge, Tennis Court Rd., Cambridge, CB2 1QW, UK

关键词: Drosophila Toll receptor;    Leucine-rich repeat peptide;    Circular dichroism spectroscopy;    Secondary structure;   

DOI  :  10.1016/0014-5793(91)81110-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Leucine-rich repeats (LRRs) are 22–28 amino acid-long sequence motifs found in a family of cytoplasmic, membrane and extracellular proteins. There is evidence that LRRs function in signal transduction, cellular adhesion and protein-protein interactions. Here we report unusual properties of a synthetic LRR peptide derived from the sequence of the Drosophila membrane receptor Toll. In neutral solution the peptide forms a gel revealed by electron microscopy to consist of extended filaments approximately 8 nm in thickness. As the gel forms, the circular dichroism spectrum of the peptide solution changes from one characteristic of random coil to one associated with β-sheet structures. Molecular modelling suggests that the peptides form an amphipathic structure with a predominantly apolar and charged surface. Based on these results, models for the gross structure of the peptide filaments and a possible molecular mechanism for cellular adhesion are proposed.

【 授权许可】

Unknown