Abstract:
: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 beta-sheet structures. Molecular modelling suggests that the peptide form an amphipathic structure with a predominantly apolar and charged surface. Based on these results, models for the gross structure of the peptides filaments and a possible molecular mechanism for cellular adhesion are proposed.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gay NJ,Packman LC,Weldon MA,Barna JCdoi
10.1016/0014-5793(91)81110-tkeywords:
subject
Has Abstractpub_date
1991-10-07 00:00:00pages
87-91issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(91)81110-Tjournal_volume
291pub_type
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