4j7e: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4j7e|  PDB=4j7e  |  SCENE=  }}
===The 1.63A crystal structure of humanized Xenopus MDM2 with a nutlin fragment, RO5524529===
{{ABSTRACT_PUBMED_14704432}}


The entry 4j7e is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/MDM2_XENLA MDM2_XENLA]] E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degration by the proteasome (By similarity).


Authors: Janson, C., Lukacs, C., Graves, B.
==About this Structure==
[[4j7e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J7E OCA].  


Description: The 1.63A crystal structure of humanized Xenopus MDM2 with a nutlin fragment, RO5524529
==Reference==
<ref group="xtra">PMID:014704432</ref><references group="xtra"/><references/>
[[Category: Xenopus laevis]]
[[Category: Graves, B.]]
[[Category: Janson, C.]]
[[Category: Lukacs, C.]]
[[Category: E3 ubiquitin ligase]]
[[Category: Imidazoline]]
[[Category: Ligase-antagonist complex]]
[[Category: Mdm2]]
[[Category: Nucleus]]
[[Category: P53]]
[[Category: Protein-protein interaction]]

Revision as of 20:51, 7 August 2013

Template:STRUCTURE 4j7e

The 1.63A crystal structure of humanized Xenopus MDM2 with a nutlin fragment, RO5524529

Template:ABSTRACT PUBMED 14704432

Function

[MDM2_XENLA] E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degration by the proteasome (By similarity).

About this Structure

4j7e is a 1 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA.

Reference

  1. Vassilev LT, Vu BT, Graves B, Carvajal D, Podlaski F, Filipovic Z, Kong N, Kammlott U, Lukacs C, Klein C, Fotouhi N, Liu EA. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science. 2004 Feb 6;303(5659):844-8. Epub 2004 Jan 2. PMID:14704432 doi:10.1126/science.1092472

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