FEBS Letters | |
A leucine‐rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a β‐sheet structure | |
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
【 预 览 】
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RO201912020295421ZK.pdf | 1011KB | download |