Acta Crystallographica Section D

Biological Crystallography

Volume 58, Part 6 Number 2 (June 2002)

short communications

Acta Cryst. (2002). D58, 1077-1080 [ doi:10.1107/S090744490200522X ]

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

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

Abstract: 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.

PDB reference: 1kn3

Keywords: PEBPs.