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J Am Chem Soc. 2008 Nov 12;130(45):14918-9. doi: 10.1021/ja805576n. Epub 2008 Oct 21.

Characterization of a conserved "threonine clasp" in CAP-Gly domains: role of a functionally critical OH/pi interaction in protein recognition.

Author information

1
Division of Signaling Biology, Ontario Cancer Institute, University of Toronto, 101 College Street, Toronto, Ontario, M5G 1L7, Canada. michael.plevin@ibs.fr

Abstract

XH/pi hydrogen bonds have been predicted to make important contributions to protein structure and function. NMR evidence is presented for an OH/pi interaction between a highly conserved threonine and phenylalanine pair found specifically in CAP-Gly domains associated with mictrotubule plus ends. The functional contribution of this nonclassical hydrogen bond in target peptide recognition is demonstrated via subtle point mutagenesis. The OH/pi interaction is part of a TxFxxxxW motif that comprises a conserved "threonine clasp" that defines function in CAP-Gly domains.

PMID:
18937471
DOI:
10.1021/ja805576n
[Indexed for MEDLINE]

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