2k4t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (19:10, 29 May 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2k4t.png|left|200px]]
 
-
{{STRUCTURE_2k4t| PDB=2k4t | SCENE= }}
+
==Solution structure of human VDAC-1 in LDAO micelles==
 +
<StructureSection load='2k4t' size='340' side='right'caption='[[2k4t]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2k4t]] 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=2K4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K4T 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=2k4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k4t OCA], [https://pdbe.org/2k4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k4t RCSB], [https://www.ebi.ac.uk/pdbsum/2k4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k4t ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/VDAC1_HUMAN VDAC1_HUMAN] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:11845315</ref> <ref>PMID:15033708</ref> <ref>PMID:18755977</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k4/2k4t_consurf.spt"</scriptWhenChecked>
 +
<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=2k4t ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The voltage-dependent anion channel (VDAC) mediates trafficking of small molecules and ions across the eukaryotic outer mitochondrial membrane. VDAC also interacts with antiapoptotic proteins from the Bcl-2 family, and this interaction inhibits release of apoptogenic proteins from the mitochondrion. We present the nuclear magnetic resonance (NMR) solution structure of recombinant human VDAC-1 reconstituted in detergent micelles. It forms a 19-stranded beta barrel with the first and last strand parallel. The hydrophobic outside perimeter of the barrel is covered by detergent molecules in a beltlike fashion. In the presence of cholesterol, recombinant VDAC-1 can form voltage-gated channels in phospholipid bilayers similar to those of the native protein. NMR measurements revealed the binding sites of VDAC-1 for the Bcl-2 protein Bcl-x(L), for reduced beta-nicotinamide adenine dinucleotide, and for cholesterol. Bcl-x(L) interacts with the VDAC barrel laterally at strands 17 and 18.
-
===Solution structure of human VDAC-1 in LDAO micelles===
+
Solution structure of the integral human membrane protein VDAC-1 in detergent micelles.,Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G Science. 2008 Aug 29;321(5893):1206-10. PMID:18755977<ref>PMID:18755977</ref>
-
{{ABSTRACT_PUBMED_18755977}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2k4t" style="background-color:#fffaf0;"></div>
-
[[2k4t]] is a 1 chain structure of [[Porin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K4T OCA].
+
==See Also==
==See Also==
-
*[[Porin|Porin]]
+
*[[Ion channels 3D structures|Ion channels 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:018755977</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Colombini, M.]]
+
[[Category: Large Structures]]
-
[[Category: Garces, R G.]]
+
[[Category: Colombini M]]
-
[[Category: Hiller, S.]]
+
[[Category: Garces RG]]
-
[[Category: Malia, T J.]]
+
[[Category: Hiller S]]
-
[[Category: Orekhov, V Y.]]
+
[[Category: Malia TJ]]
-
[[Category: Wagner, G.]]
+
[[Category: Orekhov VY]]
-
[[Category: Apoptosis]]
+
[[Category: Wagner G]]
-
[[Category: Host-virus interaction]]
+
-
[[Category: Ion transport]]
+
-
[[Category: Membrane]]
+
-
[[Category: Membrane protein]]
+
-
[[Category: Mitochondrion]]
+
-
[[Category: Outer membrane]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Porin]]
+
-
[[Category: Transmembrane]]
+
-
[[Category: Transport protein]]
+

Current revision

Solution structure of human VDAC-1 in LDAO micelles

PDB ID 2k4t

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k4t"
Personal tools