Structural highlights
Publication Abstract from PubMed
This work presents a protein structure that has been designed purely for aesthetic reasons, symbolizing decades of coiled-coil research and praising its most fundamental model system, the GCN4 leucine zipper. The GCN4 leucine zipper is a highly stable coiled coil which can be tuned to adopt different oligomeric states via mutation of its core residues. For these reasons it is used in structural studies as a stabilizing fusion adaptor. On the occasion of the 50th birthday of Andrei N. Lupas, we used it to create the first personalized protein structure: we fused the sequence ANDREI-N-LVPAS in heptad register to trimeric GCN4 adaptors and determined its structure by X-ray crystallography. The structure demonstrates the robustness and versatility of GCN4 as a fusion adaptor. We learn how proline can be accommodated in trimeric coiled coils, and put the structure into the context of the other GCN4-fusion structures known to date.
Your personalized protein structure: Andrei N. Lupas fused to GCN4 adaptors.,Deiss S, Hernandez Alvarez B, Bar K, Ewers CP, Coles M, Albrecht R, Hartmann MD J Struct Biol. 2014 Jan 29. pii: S1047-8477(14)00024-0. doi:, 10.1016/j.jsb.2014.01.013. PMID:24486584[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Deiss S, Hernandez Alvarez B, Bar K, Ewers CP, Coles M, Albrecht R, Hartmann MD. Your personalized protein structure: Andrei N. Lupas fused to GCN4 adaptors. J Struct Biol. 2014 Jan 29. pii: S1047-8477(14)00024-0. doi:, 10.1016/j.jsb.2014.01.013. PMID:24486584 doi:https://dx.doi.org/10.1016/j.jsb.2014.01.013
