2j5d: Difference between revisions

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==NMR structure of BNIP3 transmembrane domain in lipid bicelles==
==NMR structure of BNIP3 transmembrane domain in lipid bicelles==
<StructureSection load='2j5d' size='340' side='right'caption='[[2j5d]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>
<StructureSection load='2j5d' size='340' side='right'caption='[[2j5d]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2j5d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J5D FirstGlance]. <br>
<table><tr><td colspan='2'>[[2j5d]] is a 2 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=2J5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J5D 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=2j5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5d OCA], [https://pdbe.org/2j5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j5d RCSB], [https://www.ebi.ac.uk/pdbsum/2j5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j5d 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=2j5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5d OCA], [https://pdbe.org/2j5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j5d RCSB], [https://www.ebi.ac.uk/pdbsum/2j5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j5d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/BNIP3_HUMAN BNIP3_HUMAN]] Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway.<ref>PMID:19935772</ref> <ref>PMID:22292033</ref>
[https://www.uniprot.org/uniprot/BNIP3_HUMAN BNIP3_HUMAN] Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway.<ref>PMID:19935772</ref> <ref>PMID:22292033</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arseniev, A S]]
[[Category: Arseniev AS]]
[[Category: Bocharov, E V]]
[[Category: Bocharov EV]]
[[Category: Ermolyuk, Y S]]
[[Category: Ermolyuk YS]]
[[Category: Goncharuk, M V]]
[[Category: Goncharuk MV]]
[[Category: Maslennikov, I V]]
[[Category: Maslennikov IV]]
[[Category: Pustovalova, Y E]]
[[Category: Pustovalova YE]]
[[Category: Volynsky, P E]]
[[Category: Volynsky PE]]
[[Category: Apoptosis]]
[[Category: Bcl-2]]
[[Category: Bnip3]]
[[Category: Homodimer]]
[[Category: Membrane]]
[[Category: Membrane protein]]
[[Category: Mitochondrion]]
[[Category: Transmembrane]]
[[Category: Transmembrane domain]]