The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family.
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.
Simister
P C
PC
Department of Biochemistry, University of Bristol, Bristol BS8 1TD, England.
Banfield
M J
MJ
Brady
R L
RL
D000595:Amino Acid Sequence; D000727:Androgen-Binding Protein; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D049488:Phosphatidylethanolamine Binding Protein; D049294:Phospholipid Transfer Proteins; D060789:Prostatein; D011487:Protein Conformation; D060765:Secretoglobins; D017386:Sequence Homology, Amino Acid; D014598:Uteroglobin; D060788:Mammaglobin B
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D049488:Phosphatidylethanolamine Binding Protein; D049294:Phospholipid Transfer Proteins; D060789:Prostatein; D060765:Secretoglobins; D014598:Uteroglobin; C511482:PEBP1 protein, human; C511484:Scgb1d2 protein, rat; C511483:Scgb1d4 protein, rat; C556468:Scgb2a1 protein, rat; D060788:Mammaglobin B