Structural highlights
Publication Abstract from PubMed
Stable and reactive: A crystal structure at 1.35 A of a thioester coiled-coil protein reveals high similarity to all-peptide-bond proteins. In these assemblies, the thioester bonds are kept reactive towards thiol molecules in the mixture. This enables efficient domain exchange between proteins in response to changes in folding conditions or introduction of external templates.
A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry.,Dadon Z, Samiappan M, Shahar A, Zarivach R, Ashkenasy G Angew Chem Int Ed Engl. 2013 Sep 16;52(38):9944-7. doi: 10.1002/anie.201303900., Epub 2013 Aug 8. PMID:23929823[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dadon Z, Samiappan M, Shahar A, Zarivach R, Ashkenasy G. A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry. Angew Chem Int Ed Engl. 2013 Sep 16;52(38):9944-7. doi: 10.1002/anie.201303900., Epub 2013 Aug 8. PMID:23929823 doi:http://dx.doi.org/10.1002/anie.201303900
