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.


2jgz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2jgz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2jgz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2jgz| PDB=2jgz | SCENE= }}
{{STRUCTURE_2jgz| PDB=2jgz | SCENE= }}
-
'''CRYSTAL STRUCTURE OF PHOSPHO-CDK2 IN COMPLEX WITH CYCLIN B'''
+
===CRYSTAL STRUCTURE OF PHOSPHO-CDK2 IN COMPLEX WITH CYCLIN B===
-
==Overview==
+
<!--
-
The transitions of the cell cycle are regulated by the cyclin dependent protein kinases (CDKs). The cyclins activate their respective CDKs and confer substrate recognition properties. We report the structure of phospho-CDK2/cyclin B and show that cyclin B confers M phase-like properties on CDK2, the kinase that is usually associated with S phase. Cyclin B produces an almost identical activated conformation of CDK2 as that produced by cyclin A. There are differences between cyclin A and cyclin B at the recruitment site, which in cyclin A is used to recruit substrates containing an RXL motif. Because of sequence differences this site in cyclin B binds RXL motifs more weakly than in cyclin A. Despite similarity in kinase structures, phospho-CDK2/cyclin B phosphorylates substrates, such as nuclear lamin and a model peptide derived from p107, at sequences SPXX that differ from the canonical CDK2/cyclin A substrate recognition motif, SPXK. CDK2/cyclin B phosphorylation at these non-canonical sites is not dependent on the presence of a RXL recruitment motif. The p107 peptide contains two SP motifs each followed by a non-canonical sequence of which only one site (Ser640) is phosphorylated by pCDK2/cyclin A while two sites are phosphorylated by pCDK2/cyclin B. The second site is too close to the RXL motif to allow the cyclin A recruitment site to be effective, as previous work has shown that there must be at least 16 residues between the catalytic site serine and the RXL motif. Thus the cyclins A and B in addition to their role in promoting the activatory conformational switch in CDK2, also provide differential substrate specificity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17495531}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17495531 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17495531}}
==About this Structure==
==About this Structure==
Line 41: Line 45:
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Ubl conjugation]]
[[Category: Ubl conjugation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:54:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:32:36 2008''

Revision as of 01:32, 29 July 2008

Image:2jgz.png

Template:STRUCTURE 2jgz

CRYSTAL STRUCTURE OF PHOSPHO-CDK2 IN COMPLEX WITH CYCLIN B

Template:ABSTRACT PUBMED 17495531

About this Structure

2JGZ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Cyclin B and cyclin A confer different substrate recognition properties on CDK2., Brown NR, Lowe ED, Petri E, Skamnaki V, Antrobus R, Johnson LN, Cell Cycle. 2007 Jun 1;6(11):1350-9. Epub 2007 Jun 11. PMID:17495531

Page seeded by OCA on Tue Jul 29 04:32:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jgz"
Personal tools