Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE(1-34).,Houssen WE, Wright SH, Kalverda AP, Thompson GS, Kelly SM, Jaspars M Chembiochem. 2010 Aug 16. PMID:20715266[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Houssen WE, Wright SH, Kalverda AP, Thompson GS, Kelly SM, Jaspars M. Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE(1-34). Chembiochem. 2010 Aug 16. PMID:20715266 doi:10.1002/cbic.201000305
