Structural highlights
Function
[PEBP2_MOUSE] May bind to phospholipids. May act as serine protease inhibitor (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family.,Simister PC, Banfield MJ, Brady RL Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1077-80. Epub, 2002 May 29. PMID:12037323[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Simister PC, Banfield MJ, Brady RL. The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family. Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1077-80. Epub, 2002 May 29. PMID:12037323
