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

• Published in: Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-06, Vol.58 (6-2), p.1077-1080
• Main Authors: Simister, P. C., Banfield, M. J., Brady, R. L.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Androgen-Binding Protein; Animals; Carrier Proteins - chemistry; Carrier Proteins - genetics; Crystallization; Crystallography, X-Ray; Mice; Models, Molecular; Molecular Sequence Data; PEBPs; Phosphatidylethanolamine Binding Protein; Phospholipid Transfer Proteins; Prostatein; Protein Conformation; Secretoglobins; Sequence Homology, Amino Acid; Uteroglobin
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S090744490200522X

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.