4j3e: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4j3e|  PDB=4j3e  |  SCENE=  }}
===The 1.9A crystal structure of humanized Xenopus Mdm2 with nutlin-3a===
{{ABSTRACT_PUBMED_23400593}}


The entry 4j3e 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: Graves, B.J., Lukacs, C.M., Kammlott, R.U., Crowther, R.
==About this Structure==
[[4j3e]] 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=4J3E OCA].  


Description: The 1.9A crystal structure of humanized Xenopus Mdm2 with nutlin-3a
==Reference==
<ref group="xtra">PMID:014704432</ref><references group="xtra"/><references/>
[[Category: Xenopus laevis]]
[[Category: Crowther, R.]]
[[Category: Graves, B J.]]
[[Category: Kammlott, R U.]]
[[Category: Lukacs, C M.]]
[[Category: E3 ubiquitin ligase]]
[[Category: Imidazoline]]
[[Category: Ligase-antagonist complex]]
[[Category: Mdm2]]
[[Category: Nucleus]]
[[Category: P53]]
[[Category: Protein-protein interaction]]

Revision as of 14:31, 24 April 2013

Template:STRUCTURE 4j3e

The 1.9A crystal structure of humanized Xenopus Mdm2 with nutlin-3aThe 1.9A crystal structure of humanized Xenopus Mdm2 with nutlin-3a

Template:ABSTRACT PUBMED 23400593

FunctionFunction

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

About this StructureAbout this Structure

4j3e is a 1 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  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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