| Literature DB >> 27261771 |
Milosz Ruszkowski1, Zbigniew Dauter1.
Abstract
Cysteine residues ubiquitously stabilize tertiary and quaternary protein structure by formation of disulfide bridges. Here we investigate another linking interaction that involves sulfhydryl groups of cysteines, namely intra- and intermolecular methylene-bridges between cysteine and lysine residues. A number of crystal structures possessing such a linkage were identified in the Protein Data Bank. Inspection of the electron density maps and re-refinement of the nominated structures unequivocally confirmed the presence of Lys-CH2 -Cys bonds in several cases. Published 2016. This article is a U.S. Government work and is in the public domain in the USA.Entities:
Keywords: crosslink; cysteine; intermolecular; intramolecular; lysine; methylene bridge
Mesh:
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Year: 2016 PMID: 27261771 PMCID: PMC5338236 DOI: 10.1002/pro.2958
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725