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High‐Resolution Crystal Structure of a Lasso Peptide
Author(s) -
Nar Herbert,
Schmid Angela,
Puder Carsten,
Potterat Olivier
Publication year - 2010
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201000264
Subject(s) - peptide , lasso (programming language) , resolution (logic) , computational biology , crystallography , chemistry , computer science , biology , artificial intelligence , biochemistry , world wide web
Have I got noose for you! Lasso peptides are a growing class of bioactive peptides of microbial origin. The first crystal structure of a member of this family, the glucagon receptor antagonist BI‐32169, shows that the fold is built predominantly by regular secondary structural elements and a tight network of hydrogen bonds that are partially shielded from solvent by hydrophobic amino acid side chains. This results in an extraordinarily stable structure that is resistant to thermal unfolding or proteolytic digestion, which facilitates its biological function.