View source for 2m5i


==NMR structures of human apoptotic protein tBid in LPPG micelle==
<StructureSection load='2m5i' size='340' side='right'caption='[[2m5i]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m5i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M5I FirstGlance]. <br>
</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=2m5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m5i OCA], [https://pdbe.org/2m5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m5i RCSB], [https://www.ebi.ac.uk/pdbsum/2m5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m5i ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BID_HUMAN BID_HUMAN] The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2.<ref>PMID:14583606</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Bcl-2 family proteins regulate mitochondria mediated apoptosis through intricate molecular mechanisms. One of the pro-apoptotic proteins, tBid, can induce apoptosis by promoting Bax activation, Bax homo-oligomerization and mitochondrial outer membrane permeabilization. Association of tBid on the mitochondrial outer membrane is key to its biological function. Therefore knowing the conformation of tBid on the membrane will be the first step toward understanding its crucial role in triggering apoptosis. Here, we present the NMR characterization of the structure and dynamics of human tBid in LPPG micelles. Our data showed that tBid is monomeric with six well-defined alpha-helices in the micelles. Compared to the full-length Bid structure, a longer flexible loop between tBid helix alpha4 and alpha5 was observed. Helices in tBid do not pack into a compact fold but form an extended structure with a C-shape configuration in the micelles. All six tBid helices were shown to interact with LPPG micelles, with helix alpha6 and alpha7 being more embedded. Of note, the BH3-containing helix alpha3, which previously believed to be exposed above the membrane surface, is also membrane associated, suggesting an on-the-membrane binding mode for tBid interaction with Bax. Our data provided structural details on membrane-associated state of tBid and the functional implications of its membrane-associated BH3 domain.

Structural insights of tBid, the caspase-8 activated Bid, and its BH3 domain.,Wang Y, Tjandra N J Biol Chem. 2013 Oct 24. PMID:24158446<ref>PMID:24158446</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m5i" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Tjandra N]]
[[Category: Wang Y]]