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.


2px9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2px9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2px9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2px9| PDB=2px9 | SCENE= }}
{{STRUCTURE_2px9| PDB=2px9 | SCENE= }}
-
'''The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications'''
+
===The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications===
-
==Overview==
+
<!--
-
Ubiquitin-like modifications, which are carried out by similar biochemical mechanisms, regulate nearly every aspect of cellular function. Despite the recent advancements in characterizing their enzymology, our knowledge about the dynamic processes of these modifications is still fragmentary. In this study, we have uncovered an intrinsic affinity between the SUMO E2 and the Cys domain of SUMO E1. NMR studies in combination with paramagnetic spin labeling demonstrate that this interaction is mediated by previously unknown interfaces on both E1 and E2 and places the two catalytic Cys residues of the two enzymes in close proximity. Site-directed mutagenesis and enzymatic assays indicate that the interaction is fundamentally important for the transfer of SUMO from E1 to E2. Results from this study suggest that the interaction between E2 and the Cys domain of E1 participates in guiding the E2's translocation to E1's enzymatic active site in ubiquitin-like modifications.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17643372}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17643372 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17643372}}
==About this Structure==
==About this Structure==
-
2PX9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PX9 OCA].
+
2PX9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PX9 OCA].
==Reference==
==Reference==
Line 37: Line 41:
[[Category: Ubc9]]
[[Category: Ubc9]]
[[Category: Ubiquitination]]
[[Category: Ubiquitination]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:57:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:01:22 2008''

Revision as of 05:01, 29 July 2008

Image:2px9.png

Template:STRUCTURE 2px9

The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications

Template:ABSTRACT PUBMED 17643372

About this Structure

2PX9 is a Protein complex structure of sequences from Homo sapiens. Full experimental information is available from OCA.

Reference

The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications., Wang J, Hu W, Cai S, Lee B, Song J, Chen Y, Mol Cell. 2007 Jul 20;27(2):228-37. PMID:17643372

Page seeded by OCA on Tue Jul 29 08:01:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2px9"
Personal tools