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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Banfield MJ,Brady RLdoi
10.1006/jmbi.2000.3619keywords:
subject
Has Abstractpub_date
2000-04-14 00:00:00pages
1159-70issue
5eissn
0022-2836issn
1089-8638pii
S0022-2836(00)93619-2journal_volume
297pub_type
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