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Publication Abstract from PubMed

The parasite Cryptosporidium parvum has three 14-3-3 proteins: Cp14epsilon, Cp14a and Cp14b, with only Cp14epsilon similar to human 14-3-3 proteins in sequence, peptide-binding properties and structure. Structurally, Cp14a features the classical 14-3-3 dimer but with a uniquely wide pocket and a disoriented RRY triad potentially incapable of binding phosphopeptides. The Cp14b protein deviates from the norm significantly: (i) In one subunit, the phosphorylated C-terminal tail is bound in the binding groove like a phosphopeptide. This supports our binding study indicating this protein was stabilized by a peptide mimicking its last six residues. (ii) The other subunit has eight helices instead of nine, with alphaA and alphaB forming a single helix and occluding the peptide-binding cleft. (iii) The protein forms a degenerate dimer with the two binding grooves divided and facing opposite directions. These features conspire to block and disrupt the bicameral substrate-binding pocket, suggesting a possible tripartite auto-regulation mechanism that has not been observed previously. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.

Characterization of 14-3-3 proteins from Cryptosporidium parvum.,Brokx SJ, Wernimont AK, Dong A, Wasney GA, Lin YH, Lew J, Vedadi M, Lee WH, Hui R PLoS One. 2011;6(8):e14827. Epub 2011 Aug 11. PMID:21853016^[1]

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