1KN3
Murine PEBP-2 (phosphatidylethanolamine-binding protein-2)
Summary for 1KN3
| Entry DOI | 10.2210/pdb1kn3/pdb |
| Related | 1A44 1BD9 1BEH 1FJJ 1FUX 1QOU |
| Descriptor | Phosphatidylethanolamine Binding Protein-2 (2 entities in total) |
| Functional Keywords | phosphatidylethanolamine binding, raf-1 kinase inhibitor, cis-peptide, protein binding |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm: Q8VIN1 |
| Total number of polymer chains | 1 |
| Total formula weight | 20777.60 |
| Authors | Simister, P.C.,Banfield, M.J.,Brady, R.L. (deposition date: 2001-12-18, release date: 2002-06-12, Last modification date: 2023-08-16) |
| Primary citation | Simister, P.C.,Banfield, M.J.,Brady, R.L. The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family. Acta Crystallogr.,Sect.D, 58:1077-1080, 2002 Cited by PubMed 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. PubMed: 12037323DOI: 10.1107/S090744490200522X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
