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Publication Abstract from PubMed

The structure of a putative Raf kinase inhibitor protein (RKIP) homolog from the eukaryotic parasite Plasmodium vivax has been studied to a resolution of 1.3 A using multiple-wavelength anomalous diffraction at the Se K edge. This protozoan protein is topologically similar to previously studied members of the phosphatidylethanolamine-binding protein (PEBP) sequence family, but exhibits a distinctive left-handed alpha-helical region at one side of the canonical phospholipid-binding site. Re-examination of previously determined PEBP structures suggests that the P. vivax protein and yeast carboxypeptidase Y inhibitor may represent a structurally distinct subfamily of the diverse PEBP-sequence family.

The structure of Plasmodium vivax phosphatidylethanolamine-binding protein suggests a functional motif containing a left-handed helix.,Arakaki T, Neely H, Boni E, Mueller N, Buckner FS, Van Voorhis WC, Lauricella A, DeTitta G, Luft J, Hol WG, Merritt EA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Mar 1;63(Pt, 3):178-82. Epub 2007 Feb 23. PMID:17329808^[1]

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