2ezw: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:2ezw.gif|left|200px]]
{{Seed}}
[[Image:2ezw.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ezw|  PDB=2ezw  |  SCENE=  }}  
{{STRUCTURE_2ezw|  PDB=2ezw  |  SCENE=  }}  


'''Solution structure of the docking and dimerization domain of the type I alpha regulatory subunit of protein kinase A (RIalpha D/D)'''
===Solution structure of the docking and dimerization domain of the type I alpha regulatory subunit of protein kinase A (RIalpha D/D)===




==Overview==
<!--
The subcellular localization of cAMP-dependent protein kinase (PKA) occurs through interaction with A-Kinase Anchoring Proteins (AKAPs). AKAPs bind to the PKA regulatory subunit dimer of both type Ialpha and type IIalpha (RIalpha and RIIalpha). RIalpha and RIIalpha display characteristic localization within different cell types, which is maintained by interaction of AKAPs with the N-terminal dimerization and docking domain (D/D) of the respective regulatory subunit. Previously, we reported the solution structure of RIIa D/D module, both free and bound to AKAPs. We have now solved the solution structure of the dimerization and docking domain of the type Ialpha regulatory dimer subunit (RIalpha D/D). RIalpha D/D is a compact docking module, with unusual interchain disulfide bonds that help maintain the AKAP interaction surface. In contrast to the shallow hydrophobic groove for AKAP binding across the surface of the RIIalpha D/D dimeric interface, the RIalpha D/D module presents a deep cleft for proposed AKAP binding. RIalpha and RIIalpha D/D interaction modules present drastically differing dimeric topographies, despite a conserved X-type four-helix bundle structure.
The line below this paragraph, {{ABSTRACT_PUBMED_12860132}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12860132 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12860132}}


==About this Structure==
==About this Structure==
2EZW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZW OCA].  
2EZW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZW OCA].  


==Reference==
==Reference==
Line 27: Line 31:
[[Category: Four-helix bundle]]
[[Category: Four-helix bundle]]
[[Category: Regulatory subunit]]
[[Category: Regulatory subunit]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:17:52 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:14:26 2008''

Revision as of 10:14, 27 July 2008

File:2ezw.png

Template:STRUCTURE 2ezw

Solution structure of the docking and dimerization domain of the type I alpha regulatory subunit of protein kinase A (RIalpha D/D)

Template:ABSTRACT PUBMED 12860132

About this Structure

2EZW is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

Reference

Related protein-protein interaction modules present drastically different surface topographies despite a conserved helical platform., Banky P, Roy M, Newlon MG, Morikis D, Haste NM, Taylor SS, Jennings PA, J Mol Biol. 2003 Jul 25;330(5):1117-29. PMID:12860132

Page seeded by OCA on Sun Jul 27 13:14:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2ezw&oldid=647784"