2m8s: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2m8s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M8S FirstGlance]. <br>
<table><tr><td colspan='2'>[[2m8s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M8S FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m8s OCA], [https://pdbe.org/2m8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m8s RCSB], [https://www.ebi.ac.uk/pdbsum/2m8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m8s ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m8s OCA], [https://pdbe.org/2m8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m8s RCSB], [https://www.ebi.ac.uk/pdbsum/2m8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m8s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://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>  
[https://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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The membrane form of heparin binding EGF-like growth factor (proHB-EGF) yields secreted HB-EGF and a membrane-anchored cytoplasmic tail (proHB-EGF-CT), which may be targeted to the nuclear membrane after a shedding stimulus. Bcl-2-associated athanogene 1 (BAG-1) accumulates in the nuclei and inhibits apoptosis in adenoma-derived cell lines. The maintenance of high levels of nuclear BAG-1 enhances cell survival. However, the ubiquitin homology domain of BAG-1 from Mus musculus (mBAG-1-UBH) is proposed to interact with proHB-EGF-CT, and this interaction may enhance the cytoprotection against the apoptosis inducer. The mechanism of the synergistic anti-apoptosis function of proHB-EGF-CT and mBAG-1-UBH is still unknown. We offer a hypothesis that proHB-EGF-CT can maintain high levels of nuclear BAG-1. In this study, we first report the three-dimensional nuclear magnetic resonance structure of proHB-EGF-CT complexed with mBAG-1-UBH. In the structure of the complex, the residues in the C-terminus and one turn between beta-strands beta1 and beta2 of mBAG-1-UBH bind to two terminals of proHB-EGF-CT, which folds into a loop with end-to-end contact. This end-to-end folding of proHB-EGF-CT causes the basic amino acids to colocalize and form a positively charged groove. The dominant forces in the binding interface between proHB-EGF-CT and mBAG-1-UBH are charge-charge interactions. On the basis of our mutagenesis results, the basic amino acid cluster in the N-terminus of proHB-EGF-CT is the crucial binding site for mBAG-1-UBH, whereas another basic amino acid in the C-terminus facilitates this interaction. Interestingly, the mBAG-1-UBH binding region on the proHB-EGF-CT peptide is also involved in the region found to be important for nuclear envelope targeting, supporting the hypothesis that proHB-EGF-CT is most likely able to trigger the nuclear translocation of BAG-1 in keeping its level high.
Nuclear Magnetic Resonance Structure of the Cytoplasmic Tail of Heparin Binding EGF-like Growth Factor (proHB-EGF-CT) Complexed with the Ubiquitin Homology Domain of Bcl-2-Associated Athanogene 1 from Mus musculus (mBAG-1-UBH).,Hung KW, Huang HW, Cho CC, Chang SC, Yu C Biochemistry. 2014 Apr 1;53(12):1935-46. doi: 10.1021/bi5003019. Epub 2014 Mar, 24. PMID:24628338<ref>PMID:24628338</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m8s" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 06:59, 1 May 2024

NMR Structure of the Cytoplasmic Tail of the Membrane Form of Heparin-binding EGF-like Growth Factor (proHB-EGF-CT) Complexed with the Ubiquitin Homology Domain of Bcl-2-associated Athanogene 1 from Mus musculus (mBAG-1-UBH)

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