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FOR THE RECORD

Mimicry by asx- and ST-turns of the four main types of -turn in proteins

¹ Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow, G12 8QQ, United Kingdom
² Cambridge Crystallographic Data Centre, Cambridge, CB2 1EZ, United Kingdom

(RECEIVED July 9, 2004; FINAL REVISION July 30, 2004; ACCEPTED July 30, 2004)

Hydrogen-bonded -turns in proteins occur in four categories: type I (the most common), type II, type II’, and type I’. Asx-turns resemble -turns, in that both have an NH. . .OC hydrogen bond forming a ring of 10 atoms. Serine and threonine side chains also commonly form hydrogen-bonded turns, here called ST-turns. Asx-turns and ST-turns can be categorized into four classes, based on side chain rotamers and the conformation of the central turn residue, which are geometrically equivalent to the four types of -turns. We propose asx- and ST-turns be named using the type I, II, I’, and II’ -turn nomenclature. Using this, the frequency of occurrence of both asx- and ST-turns is: type II’ > type I > type II > type I’, whereas for -turns it is type I > type II > type I’ > type II’. Almost all type II asx-turns occur as a recently described three residue feature named an asx-nest.

Keywords: asx-turn; -turn; hydrogen-bond; nest; ST-turn

Reprint requests to: E. James Milner-White, Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow, G12 8QQ, UK; e-mail: J.Milner-White{at}bio.gla.ac.uk; fax: +44-141-330-4620.

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