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.


1jad

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jad.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1jad.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jad| PDB=1jad | SCENE= }}
{{STRUCTURE_1jad| PDB=1jad | SCENE= }}
-
'''C-terminal Domain of Turkey PLC-beta'''
+
===C-terminal Domain of Turkey PLC-beta===
-
==Overview==
+
<!--
-
GTP-bound subunits of the Gq family of G alpha subunits directly activate phospholipase C-beta (PLC-beta) isozymes to produce the second messengers inositol 1,4,5-trisphosphate and diacylglycerol. PLC-betas are GTPase activating proteins (GAPs) that also promote the formation of GDP-bound, inactive G beta subunits. Both phospholipase activation by G alpha-GTP subunits and GAP activity require a C-terminal region unique to PLC-beta isozymes. The crystal structure of the C-terminal region from an avian PLC-beta, determined at 2.4 A resolution, reveals a novel fold composed almost entirely of three long helices forming a coiled-coil that dimerizes along its long axis in an antiparallel orientation. The dimer interface is extensive ( approximately 3,200 A(2)), and, based on gel exclusion chromatography, full length PLC-betas are dimeric, indicating that PLC-betas likely function as dimers. Sequence conservation, mutational data and molecular modeling show that an electrostatically positive surface of the dimer contains the major determinants for binding G beta q. Effector dimerization, as highlighted by PLC-betas, provides a viable mechanism for regulating signaling cascades linked to heterotrimeric G proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11753430}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11753430 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11753430}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Waldo, G L.]]
[[Category: Waldo, G L.]]
[[Category: Alpha helical coiled coil]]
[[Category: Alpha helical coiled coil]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:58:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:18:39 2008''

Revision as of 10:18, 27 July 2008

Template:STRUCTURE 1jad

C-terminal Domain of Turkey PLC-beta

Template:ABSTRACT PUBMED 11753430

About this Structure

1JAD is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.

Reference

A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q., Singer AU, Waldo GL, Harden TK, Sondek J, Nat Struct Biol. 2002 Jan;9(1):32-6. PMID:11753430

Page seeded by OCA on Sun Jul 27 13:18:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools