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2vgq

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[[Image:2vgq.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of Human IPS-1 CARD==
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|PDB= 2vgq |SIZE=350|CAPTION= <scene name='initialview01'>2vgq</scene>, resolution 2.10&Aring;
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<StructureSection load='2vgq' size='340' side='right'caption='[[2vgq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Mtt+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Chain+A'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Chain+A'>AC5</scene> and <scene name='pdbsite=AC6:So4+Binding+Site+For+Chain+A'>AC6</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MTT:MALTOTETRAOSE'>MTT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[2vgq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VGQ FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgq OCA], [https://pdbe.org/2vgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vgq RCSB], [https://www.ebi.ac.uk/pdbsum/2vgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vgq ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1mh3|1MH3]], [[1hsj|1HSJ]], [[1y4c|1Y4C]], [[1ezo|1EZO]], [[1fqc|1FQC]], [[1anf|1ANF]], [[1lls|1LLS]], [[3mbp|3MBP]], [[1zkb|1ZKB]], [[1mpb|1MPB]], [[1dmb|1DMB]], [[1ezp|1EZP]], [[1ez9|1EZ9]], [[1zjl|1ZJL]], [[2h25|2H25]], [[1jvx|1JVX]], [[1n3x|1N3X]], [[1nl5|1NL5]], [[1a7l|1A7L]], [[1r6z|1R6Z]], [[1zmg|1ZMG]], [[1t0k|1T0K]], [[1mh4|1MH4]], [[1jw5|1JW5]], [[1fqa|1FQA]], [[1iud|1IUD]], [[1ziu|1ZIU]], [[1mg1|1MG1]], [[1mdp|1MDP]], [[1fqb|1FQB]], [[1jw4|1JW4]], [[1omp|1OMP]], [[1n3w|1N3W]], [[1nmu|1NMU]], [[1mpd|1MPD]], [[1ytv|1YTV]], [[1mdq|1MDQ]], [[1lax|1LAX]], [[1peb|1PEB]], [[1mpc|1MPC]], [[1jvy|1JVY]], [[1fqd|1FQD]], [[1svx|1SVX]], [[2d21|2D21]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgq OCA], [http://www.ebi.ac.uk/pdbsum/2vgq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vgq RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/MAVS_HUMAN MAVS_HUMAN] Required for innate immune defense against viruses. Acts downstream of DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis.<ref>PMID:16125763</ref> <ref>PMID:16153868</ref> <ref>PMID:16177806</ref> <ref>PMID:16127453</ref> <ref>PMID:19631370</ref> <ref>PMID:20451243</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vg/2vgq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2vgq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: IPS-1/MAVS/VISA/Cardif is an adaptor protein that plays a crucial role in the induction of interferons in response to viral infection. In the initial stage of the intracellular antiviral response two RNA helicases, retinoic acid inducible gene-I (RIG-I) and melanoma differentiation-association gene 5 (MDA5), are independently able to bind viral RNA in the cytoplasm. The 62 kDa protein IPS-1/MAVS/VISA/Cardif contains an N-terminal caspase activation and recruitment (CARD) domain that associates with the CARD regions of RIG-I and MDA5, ultimately leading to the induction of type I interferons. As a first step towards understanding the molecular basis of this important adaptor protein we have undertaken structural studies of the IPS-1 MAVS/VISA/Cardif CARD region. RESULTS: The crystal structure of human IPS-1/MAVS/VISA/Cardif CARD has been determined to 2.1A resolution. The protein was expressed and crystallized as a maltose-binding protein (MBP) fusion protein. The MBP and IPS-1 components each form a distinct domain within the structure. IPS-1/MAVS/VISA/Cardif CARD adopts a characteristic six-helix bundle with a Greek-key topology and, in common with a number of other known CARD structures, contains two major polar surfaces on opposite sides of the molecule. One face has a surface-exposed, disordered tryptophan residue that may explain the poor solubility of untagged expression constructs. CONCLUSION: The IPS-1/MAVS/VISA/Cardif CARD domain adopts the classic CARD fold with an asymmetric surface charge distribution that is typical of CARD domains involved in homotypic protein-protein interactions. The location of the two polar areas on IPS-1/MAVS/VISA/Cardif CARD suggest possible types of associations that this domain makes with the two CARD domains of MDA5 or RIG-I. The N-terminal CARD domains of RIG-I and MDA5 share greatest sequence similarity with IPS-1/MAVS/VISA/Cardif CARD and this has allowed modelling of their structures. These models show a very different charge profile for the equivalent surfaces compared to IPS-1/MAVS/VISA/Cardif CARD.
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'''CRYSTAL STRUCTURE OF HUMAN IPS-1 CARD'''
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Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain.,Potter JA, Randall RE, Taylor GL BMC Struct Biol. 2008 Feb 28;8:11. PMID:18307765<ref>PMID:18307765</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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2VGQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_homo_sapiens Escherichia coli, homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGQ OCA].
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<div class="pdbe-citations 2vgq" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia coli, homo sapiens]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Potter, J A.]]
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__TOC__
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[[Category: Randall, R E.]]
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</StructureSection>
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[[Category: Taylor, G L.]]
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[[Category: Escherichia coli]]
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[[Category: caspase activation]]
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[[Category: Homo sapiens]]
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[[Category: caspase recruitment domain]]
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[[Category: Large Structures]]
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[[Category: chimera]]
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[[Category: Potter JA]]
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[[Category: fusion protein]]
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[[Category: Randall RE]]
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[[Category: immune system]]
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[[Category: Taylor GL]]
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[[Category: immune system/transport complex]]
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[[Category: innate immunity]]
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[[Category: ips1/mavs/visa/cardif]]
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[[Category: sugar transport]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:12:01 2008''
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Current revision

Crystal Structure of Human IPS-1 CARD

PDB ID 2vgq

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