2bid: Difference between revisions

No edit summary
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2bid.jpg|left|200px]]


{{Structure
==HUMAN PRO-APOPTOTIC PROTEIN BID==
|PDB= 2bid |SIZE=350|CAPTION= <scene name='initialview01'>2bid</scene>
<StructureSection load='2bid' size='340' side='right'caption='[[2bid]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2bid]] 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=2BID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BID FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bid OCA], [https://pdbe.org/2bid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bid RCSB], [https://www.ebi.ac.uk/pdbsum/2bid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bid ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bid OCA], [http://www.ebi.ac.uk/pdbsum/2bid PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bid RCSB]</span>
[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>
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''HUMAN PRO-APOPTOTIC PROTEIN BID'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/2bid_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bid ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage.
We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage.


==About this Structure==
Solution structure of BID, an intracellular amplifier of apoptotic signaling.,Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G Cell. 1999 Mar 5;96(5):615-24. PMID:10089877<ref>PMID:10089877</ref>
2BID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BID OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of BID, an intracellular amplifier of apoptotic signaling., Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G, Cell. 1999 Mar 5;96(5):615-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089877 10089877]
</div>
<div class="pdbe-citations 2bid" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chou, J J.]]
[[Category: Chou JJ]]
[[Category: Li, H.]]
[[Category: Li H]]
[[Category: Salvesen, G S.]]
[[Category: Salvesen GS]]
[[Category: Wagner, G.]]
[[Category: Wagner G]]
[[Category: Yuan, J.]]
[[Category: Yuan J]]
[[Category: apoptosis regulation and amplification]]
[[Category: programmed cell death]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:06:53 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA