Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KN3

Murine PEBP-2 (phosphatidylethanolamine-binding protein-2)

Summary for 1KN3
Entry DOI10.2210/pdb1kn3/pdb
Related1A44 1BD9 1BEH 1FJJ 1FUX 1QOU
DescriptorPhosphatidylethanolamine Binding Protein-2 (2 entities in total)
Functional Keywordsphosphatidylethanolamine binding, raf-1 kinase inhibitor, cis-peptide, protein binding
Biological sourceMus musculus (house mouse)
Cellular locationCytoplasm: Q8VIN1
Total number of polymer chains1
Total formula weight20777.60
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 citationSimister, 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: 12037323
DOI: 10.1107/S090744490200522X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

243531

数据于2025-10-22公开中

PDB statisticsPDBj update infoContact PDBjnumon