1QOU
CEN (Centroradialis) protein from Antirrhinum
Summary for 1QOU
| Entry DOI | 10.2210/pdb1qou/pdb |
| Descriptor | CEN (2 entities in total) |
| Functional Keywords | plant protein, influorescence determination in flowering plant meristem, signalling, member of the phosphatidylethanolamine binding protein family |
| Biological source | ANTIRRHINUM MAJUS (GARDEN SNAPDRAGON) |
| Cellular location | Cytoplasm: Q41261 |
| Total number of polymer chains | 2 |
| Total formula weight | 40700.56 |
| Authors | Banfield, M.J.,Brady, R.L. (deposition date: 1999-11-17, release date: 2000-03-31, Last modification date: 2024-11-20) |
| Primary citation | Banfield, M.J.,Brady, R.L. The Structure of Antirrhinum Centroradialis Protein (Cen) Suggests a Role as a Kinase Regulator J.Mol.Biol., 297:1161-, 2000 Cited by PubMed Abstract: Expression of the plant protein centroradialis (CEN) leads to a morphological switch between shoot growth and the development of flower structures (inflorescence). We have determined the crystal structure of Antirrhinum CEN to 1.9 A resolution. This structure confirms the CEN proteins as a subset of the family of phosphatidylethanolamine-binding proteins (PEBP), as predicted from sequence homology. Mammalian forms of PEBP have been found to act as inhibitors of MAP kinase signalling, a central signalling cascade regulating cell differentiation. CEN and PEBP proteins share a similar topology dominated by a large central beta-sheet. The strong conservation of a binding pocket at one end of this sheet which is capable of binding phosphoryl ligands, suggests the biological effects of CEN, like PEBP, arise from the ability of this region to form complexes with phosphorylated ligands, hence interfering with kinases and their effectors. PubMed: 10764580DOI: 10.1006/JMBI.2000.3619 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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