2lwp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_2lwp| PDB=2lwp | SCENE= }}
 +
===The NMR solution structure of the the ubiquitin homology domain of mouse BAG-1===
 +
{{ABSTRACT_PUBMED_23277101}}
-
The entry 2lwp is ON HOLD until Paper Publication
+
==Function==
 +
[[http://www.uniprot.org/uniprot/BAG1_MOUSE BAG1_MOUSE]] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.<ref>PMID:9873016</ref>
-
Authors: Huang, H., Yu, C.
+
==About this Structure==
 +
[[2lwp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LWP OCA].
-
Description: The NMR solution structure of the the ubiquitin homology domain of mouse BAG-1
+
==Reference==
 +
<ref group="xtra">PMID:023277101</ref><references group="xtra"/><references/>
 +
[[Category: Mus musculus]]
 +
[[Category: Huang, H.]]
 +
[[Category: Yu, C.]]
 +
[[Category: Apoptosis]]
 +
[[Category: Proteasomal degradation]]

Revision as of 17:59, 19 June 2013

Template:STRUCTURE 2lwp

Contents

The NMR solution structure of the the ubiquitin homology domain of mouse BAG-1

Template:ABSTRACT PUBMED 23277101

Function

[BAG1_MOUSE] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.[1]

About this Structure

2lwp is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA.

Reference

  • Huang HW, Yu C. The NMR solution structure of the ubiquitin homology domain of Bcl-2-associated athanogene 1 (BAG-1-UBH) from Mus musculus. Biochem Biophys Res Commun. 2013 Feb 1;431(1):86-91. doi:, 10.1016/j.bbrc.2012.12.082. Epub 2012 Dec 28. PMID:23277101 doi:10.1016/j.bbrc.2012.12.082
  1. Takayama S, Xie Z, Reed JC. An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators. J Biol Chem. 1999 Jan 8;274(2):781-6. PMID:9873016

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools