Abstract
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.
Publication types
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Comparative Study
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Motifs / physiology
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Amino Acid Sequence
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Animals
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Binding Sites / physiology
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Crystallography, X-Ray
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Molecular Sequence Data
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Phosphatidylethanolamine Binding Protein / chemistry*
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Phosphatidylethanolamine Binding Protein / metabolism
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Phosphatidylethanolamine Binding Protein / physiology*
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Plasmodium vivax / chemistry*
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Plasmodium vivax / metabolism
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Protein Conformation
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Protein Kinase Inhibitors / chemistry
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Protein Kinase Inhibitors / metabolism
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Protein Structure, Secondary / physiology
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Protozoan Proteins / chemistry
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Protozoan Proteins / metabolism
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Protozoan Proteins / physiology
Substances
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Phosphatidylethanolamine Binding Protein
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Protein Kinase Inhibitors
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Protozoan Proteins