The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family

P. C. Simister, M. J. Banfield, R. L. Brady*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

64 Citations (Scopus)


Proteins from the PEBP (phosphatidylethanolamine-binding protein) family have been identified in a wide variety of species and are thought to regulate a range of intracellular signalling cascades. The rat homologue (known as RKIP; Raf-1 kinase inhibitor protein) has been shown to negatively regulate the MAP kinase pathway through formation of inhibitory complexes with Raf-1 and MEK. The crystal structure of a new, murine member of the PEBP family, termed mPEBP-2, has been determined. On the basis of amino-acid homology, mPEBP-2 belongs to a distinct subset of the mammalian PEBP proteins. Nonetheless, mPEBP-2 is seen to be very similar in structure to other PEBP proteins from human, bovine and plant sources. Regions of distinctive sequence associated with the PEBP-2 subset are discussed with reference to this structure.

Original languageEnglish
Pages (from-to)1077-1080
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Issue number6 II
Publication statusPublished - 1 Jan 2002

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