This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1r2a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1r2a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1r2a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1r2a| PDB=1r2a | SCENE= }}
{{STRUCTURE_1r2a| PDB=1r2a | SCENE= }}
-
'''THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR'''
+
===THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR===
-
==Overview==
+
<!--
-
Compartmentalization of signal transduction enzymes into signaling complexes is an important mechanism to ensure the specificity of intracellular events. Formation of these complexes is mediated by specialized protein motifs that participate in protein-protein interactions. The adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) is localized through interaction of the regulatory (R) subunit dimer with A-kinase-anchoring proteins (AKAPs). We now report the solution structure of the type II PKA R-subunit fragment RIIalpha(1-44), which encompasses both the AKAP-binding and dimerization interfaces. This structure incorporates an X-type four-helix bundle dimerization motif with an extended hydrophobic face that is necessary for high-affinity AKAP binding. NMR data on the complex between RIIalpha(1-44) and an AKAP fragment reveals extensive contacts between the two proteins. Interestingly, this same dimerization motif is present in other signaling molecules, the S100 family. Therefore, the X-type four-helix bundle may represent a conserved fold for protein-protein interactions in signal transduction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10074940}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10074940 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10074940}}
==About this Structure==
==About this Structure==
-
1R2A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2A OCA].
+
1R2A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2A OCA].
==Reference==
==Reference==
Line 33: Line 37:
[[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 Sat May 3 06:59:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:07:00 2008''

Revision as of 10:07, 28 July 2008

Image:1r2a.png

Template:STRUCTURE 1r2a

THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR

Template:ABSTRACT PUBMED 10074940

About this Structure

1R2A is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

Reference

The molecular basis for protein kinase A anchoring revealed by solution NMR., Newlon MG, Roy M, Morikis D, Hausken ZE, Coghlan V, Scott JD, Jennings PA, Nat Struct Biol. 1999 Mar;6(3):222-7. PMID:10074940

Page seeded by OCA on Mon Jul 28 13:07:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r2a"
Personal tools