2f86: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2f86.gif|left|200px]]
{{Seed}}
[[Image:2f86.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2f86|  PDB=2f86  |  SCENE=  }}  
{{STRUCTURE_2f86|  PDB=2f86  |  SCENE=  }}  


'''The Association Domain of C. elegans CaMKII'''
===The Association Domain of C. elegans CaMKII===




==Overview==
<!--
Ca2+/calmodulin activated protein kinase II (CaMKII) is an oligomeric protein kinase with a unique holoenyzme architecture. The subunits of CaMKII are bound together into the holoenzyme by the association domain, a C-terminal region of approximately 140 residues in the CaMKII polypeptide. Single particle analyses of electron micrographs have suggested previously that the holoenyzme forms a dodecamer that contains two stacked 6-fold symmetric rings. In contrast, a recent crystal structure of the isolated association domain of mouse CaMKIIalpha has revealed a tetradecameric assembly with two stacked 7-fold symmetric rings. In this study, we have determined the crystal structure of the Caenorhabditis elegans CaMKII association domain and it too forms a tetradecamer. We also show by electron microscopy that in its fully assembled form the CaMKII holoenzyme is a dodecamer but without the kinase domains, either from expression of the isolated association domain in bacteria or following their removal by proteolysis, the association domains form a tetradecamer. We speculate that the holoenzyme is held in its 6-fold symmetric state by the interactions of the N-terminal approximately 1-335 residues and that the removal of this region allows the association domain to convert into a more stable 7-fold symmetric form.
The line below this paragraph, {{ABSTRACT_PUBMED_16441656}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16441656 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16441656}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Oligomerization domain]]
[[Category: Oligomerization domain]]
[[Category: Unc-43]]
[[Category: Unc-43]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:34:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:01:27 2008''

Revision as of 15:01, 27 July 2008

File:2f86.png

Template:STRUCTURE 2f86

The Association Domain of C. elegans CaMKII

Template:ABSTRACT PUBMED 16441656

About this Structure

2F86 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II., Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J, FEBS J. 2006 Feb;273(4):682-94. PMID:16441656

Page seeded by OCA on Sun Jul 27 18:01:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2f86&oldid=659613"