| Literature DB >> 20715266 |
Wael E Houssen1, Stephen H Wright, Arnout P Kalverda, Gary S Thompson, Sharon M Kelly, Marcel Jaspars.
Abstract
The solution structure of the leader sequence of the patellamide precursor peptide was analysed by using CD and determined with NOE-restrained molecular dynamics calculations. This leader sequence is highly conserved in the precursor peptides of some other cyanobactins harbouring heterocycles, and is assumed to play a role in targeting the precursor peptide to the post-translational machinery. The sequence was observed to form an alpha-helix spanning residues 13-28 with a hydrophobic surface on one side of the helix. This hydrophobic surface is proposed to be the site of the initial binding with modifying enzymes.Entities:
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Year: 2010 PMID: 20715266 DOI: 10.1002/cbic.201000305
Source DB: PubMed Journal: Chembiochem ISSN: 1439-4227 Impact factor: 3.164