2ww6

Publication Abstract from PubMed

beta-Turns are secondary structure elements not only exposed on protein surfaces, but also frequently found to be buried in protein-protein interfaces. Protein engineering so far considered mainly the backbone-constraining properties of synthetic beta-turn mimics as parts of surface-exposed loops. A beta-turn mimic, Hot horizontal lineTap, that is available in gram amounts, provides two hydroxyl groups that enhance its turn-inducing properties besides being able to form side-chain-like interactions. NMR studies on cyclic hexapeptides harboring the Hot horizontal lineTap dipeptide proved its strong beta-turn-inducing capability. Crystallographic analyses of the trimeric fibritin-foldon/Hot horizontal lineTap hybrid reveal at atomic resolution how Hot horizontal lineTap replaces a betaI'-turn by a betaII'-type structure. Furthermore, Hot horizontal lineTap adapts to the complex protein environment by participating in several direct and water-bridged interactions across the foldon trimer interface. As building blocks, beta-turn mimics capable of both backbone and side-chain mimicry may simplify the design of synthetic proteins.

Structural characterization of a beta-turn mimic within a protein-protein interface.,Eckhardt B, Grosse W, Essen LO, Geyer A Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18336-41. Epub 2010 Oct 11. PMID:20937907^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.