1qou
From Proteopedia
(New page: 200px<br /><applet load="1qou" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qou, resolution 1.9Å" /> '''CEN (CENTRORADIALIS) ...) |
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| - | [[Image:1qou.gif|left|200px]]<br /><applet load="1qou" size=" | + | [[Image:1qou.gif|left|200px]]<br /><applet load="1qou" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qou, resolution 1.9Å" /> | caption="1qou, resolution 1.9Å" /> | ||
'''CEN (CENTRORADIALIS) PROTEIN FROM ANTIRRHINUM'''<br /> | '''CEN (CENTRORADIALIS) PROTEIN FROM ANTIRRHINUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Expression of the plant protein centroradialis (CEN) leads to a | + | 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== | ==About this Structure== | ||
| - | 1QOU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Antirrhinum_majus Antirrhinum majus]. Full crystallographic information is available from [http:// | + | 1QOU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Antirrhinum_majus Antirrhinum majus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Antirrhinum majus]] | [[Category: Antirrhinum majus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Banfield, M | + | [[Category: Banfield, M J.]] |
| - | [[Category: Brady, R | + | [[Category: Brady, R L.]] |
[[Category: influorescence determination in flowering plant meristem]] | [[Category: influorescence determination in flowering plant meristem]] | ||
[[Category: member of the phosphatidylethanolamine binding protein family]] | [[Category: member of the phosphatidylethanolamine binding protein family]] | ||
[[Category: signalling]] | [[Category: signalling]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:03 2008'' |
Revision as of 12:42, 21 February 2008
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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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