2vgq
From Proteopedia
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| - | [[ | + | ==CRYSTAL STRUCTURE OF HUMAN IPS-1 CARD== |
| + | <StructureSection load='2vgq' size='340' side='right' caption='[[2vgq]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2vgq]] is a 1 chain structure with 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=2VGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VGQ FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MTT:MALTOTETRAOSE'>MTT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[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]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2vgq RCSB], [http://www.ebi.ac.uk/pdbsum/2vgq PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == 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/vg/2vgq_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Potter, J A.]] | [[Category: Potter, J A.]] | ||
Revision as of 08:14, 29 September 2014
CRYSTAL STRUCTURE OF HUMAN IPS-1 CARD
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