We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1a25

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a25.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1a25.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a25| PDB=1a25 | SCENE= }}
{{STRUCTURE_1a25| PDB=1a25 | SCENE= }}
-
'''C2 DOMAIN FROM PROTEIN KINASE C (BETA)'''
+
===C2 DOMAIN FROM PROTEIN KINASE C (BETA)===
-
==Overview==
+
<!--
-
BACKGROUND: Conventional isoforms (alpha, beta and gamma) of protein kinase C (PKC) are synergistically activated by phosphatidylserine and Ca2+; both bind to C2 domains located within the PKC amino-terminal regulatory regions. C2 domains contain a bipartite or tripartite Ca2+-binding site formed by opposing loops at one end of the protein. Neither the structural basis for cooperativity between phosphatidylserine and Ca2+, nor the binding site for phosphatidylserine are known. RESULTS: The structure of the C2 domain from PKCbeta complexed with Ca2+ and o-phospho-L-serine has been determined to 2.7 A resolution using X-ray crystallography. The eight-stranded, Greek key beta-sandwich fold of PKCbeta-C2 is similar to that of the synaptotagmin I type I C2 domain. Three Ca2+ ions, one at a novel site, were located, each sharing common aspartate ligands. One of these ligands is donated by a dyad-related C2 molecule. A phosphoserine molecule binds to a lysine-rich cluster in C2. CONCLUSIONS: Shared ligation among the three Ca2+ ions suggests that they bind cooperatively to PKCbeta-C2. Cooperativity may be compromised by the accumulation of positive charge in the binding site as successive ions are bound. Model building shows that the C1 domain could provide carboxylate and carbonyl ligands for two of the three Ca2+ sites. Ca2+-mediated interactions between the two domains could contribute to enzyme activation as well as to the creation of a positively charged phosphatidylserine-binding site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9817842}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9817842 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9817842}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Calcium++/phospholipid binding protein]]
[[Category: Calcium++/phospholipid binding protein]]
[[Category: Calcium-binding protein]]
[[Category: Calcium-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:41:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:49:58 2008''

Revision as of 12:49, 30 June 2008

Image:1a25.png

Template:STRUCTURE 1a25

C2 DOMAIN FROM PROTEIN KINASE C (BETA)

Template:ABSTRACT PUBMED 9817842

About this Structure

1A25 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+., Sutton RB, Sprang SR, Structure. 1998 Nov 15;6(11):1395-405. PMID:9817842

Page seeded by OCA on Mon Jun 30 15:49:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a25"
Personal tools