1qou

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qou OCA], [http://www.ebi.ac.uk/pdbsum/1qou PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qou RCSB]</span>
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[[Category: signalling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:16:51 2008''

Revision as of 20:16, 30 March 2008


PDB ID 1qou

Drag the structure with the mouse to rotate
, resolution 1.9Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CEN (CENTRORADIALIS) PROTEIN FROM ANTIRRHINUM


Overview

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.

About this Structure

1QOU is a Single protein structure of sequence from Antirrhinum majus. Full crystallographic information is available from OCA.

Reference

The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator., Banfield MJ, Brady RL, J Mol Biol. 2000 Apr 14;297(5):1159-70. PMID:10764580

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