Structural highlights
Publication Abstract from PubMed
The de novo design of protein-binding peptides is challenging because it requires the identification of both a sequence and a backbone conformation favorable for binding. We used a computational strategy that iterates between structure and sequence optimization to redesign the C-terminal portion of the RGS14 GoLoco motif peptide so that it adopts a new conformation when bound to Galpha(i1). An X-ray crystal structure of the redesigned complex closely matches the computational model, with a backbone root-mean-square deviation of 1.1 A.
Computational design of the sequence and structure of a protein-binding peptide.,Sammond DW, Bosch DE, Butterfoss GL, Purbeck C, Machius M, Siderovski DP, Kuhlman B J Am Chem Soc. 2011 Mar 30;133(12):4190-2. Epub 2011 Mar 9. PMID:21388199[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sammond DW, Bosch DE, Butterfoss GL, Purbeck C, Machius M, Siderovski DP, Kuhlman B. Computational design of the sequence and structure of a protein-binding peptide. J Am Chem Soc. 2011 Mar 30;133(12):4190-2. Epub 2011 Mar 9. PMID:21388199 doi:10.1021/ja110296z
