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5gqq

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Structure of ALG-2/HEBP2 Complex

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Retrieved from "http://52.214.119.220/wiki/index.php/5gqq"

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 ==Structure of ALG-2/HEBP2 Complex==
-<StructureSection load='5gqq' size='340' side='right' caption='[[5gqq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='5gqq' size='340' side='right'caption='[[5gqq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5gqq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GQQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GQQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5gqq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GQQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gqq OCA], [http://pdbe.org/5gqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gqq RCSB], [http://www.ebi.ac.uk/pdbsum/5gqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gqq ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5gqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gqq OCA], [https://pdbe.org/5gqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gqq RCSB], [https://www.ebi.ac.uk/pdbsum/5gqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gqq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEBP2_HUMAN HEBP2_HUMAN]] Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin.<ref>PMID:17098234</ref>  [[http://www.uniprot.org/uniprot/PDCD6_HUMAN PDCD6_HUMAN]] Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. May mediate Ca(2+)-regulated signals along the death pathway (By similarity). Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity.<ref>PMID:16132846</ref> <ref>PMID:19520058</ref>
+[https://www.uniprot.org/uniprot/HEBP2_HUMAN HEBP2_HUMAN] Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions. Does not bind hemin.<ref>PMID:17098234</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-In the HIV-1 replication cycle, the endosomal sorting complex required for transport (ESCRT) machinery promotes viral budding and release in the late stages. In this process, the ESCRT proteins, ALIX and TSG101, are recruited through interactions with HIV-1 Gag p6. ALG-2, also known as PDCD6, interacts with both ALIX and TSG101 and bridges ESCRT-III and ESCRT-I. In this study, we show that ALG-2 affects HIV-1 production negatively at both the exogenous and endogenous levels. Through a yeast two-hybrid screen, we identified HEBP2 as the binding partner of ALG-2, and we solved the crystal structure of the ALG-2.HEBP2 complex. The function of ALG-2.HEBP2 complex in HIV-1 replication was further explored. ALG-2 inhibits HIV-1 production by affecting Gag expression and distribution, and HEBP2 might aid this process by tethering ALG-2 in the cytoplasm.
-Structural and Functional Study of Apoptosis-linked Gene-2.Heme-binding Protein 2 Interactions in HIV-1 Production.,Ma J, Zhang X, Feng Y, Zhang H, Wang X, Zheng Y, Qiao W, Liu X J Biol Chem. 2016 Dec 23;291(52):26670-26685. doi: 10.1074/jbc.M116.752444. Epub , 2016 Oct 26. PMID:27784779<ref>PMID:27784779</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5gqq" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Cell death protein|Cell death protein]]
+*[[Cell death protein 3D structures|Cell death protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Feng, Y]]
+[[Category: Homo sapiens]]
-[[Category: Liu, X]]
+[[Category: Large Structures]]
-[[Category: Ma, J]]
+[[Category: Feng Y]]
-[[Category: Zhang, H]]
+[[Category: Liu X]]
-[[Category: Apoptosis]]
+[[Category: Ma J]]
-[[Category: Calcium ion]]
+[[Category: Zhang H]]
-[[Category: Complex]]
-[[Category: Ef hand]]

5gqq

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Structure of ALG-2/HEBP2 Complex

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