2vgq

From Proteopedia

(Difference between revisions)

Revision as of 12:16, 8 February 2016

CRYSTAL STRUCTURE OF HUMAN IPS-1 CARD

Structural highlights

2vgq is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1mh3, 1hsj, 1y4c, 1ezo, 1fqc, 1anf, 1lls, 3mbp, 1zkb, 1mpb, 1dmb, 1ezp, 1ez9, 1zjl, 2h25, 1jvx, 1n3x, 1nl5, 1a7l, 1r6z, 1zmg, 1t0k, 1mh4, 1jw5, 1fqa, 1iud, 1ziu, 1mg1, 1mdp, 1fqb, 1jw4, 1omp, 1n3w, 1nmu, 1mpd, 1ytv, 1mdq, 1lax, 1peb, 1mpc, 1jvy, 1fqd, 1svx, 2d21
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Potter JA, Randall RE, Taylor GL. Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain. BMC Struct Biol. 2008 Feb 28;8:11. PMID:18307765 doi:1472-6807-8-11

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vgq"

@@ Line 2: / Line 2: @@
 <StructureSection load='2vgq' size='340' side='right' caption='[[2vgq]], [[Resolution|resolution]] 2.10&Aring;' 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>
+<table><tr><td colspan='2'>[[2vgq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 id='ligand'><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></td></tr>
 <tr id='related'><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 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=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>
+<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=2vgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgq OCA], [http://pdbe.org/2vgq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vgq RCSB], [http://www.ebi.ac.uk/pdbsum/2vgq PDBsum]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 15: / Line 15: @@
     <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].
+</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].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2vgq" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Potter, J A]]
 [[Category: Randall, R E]]

2vgq

From Proteopedia

Revision as of 12:16, 8 February 2016

CRYSTAL STRUCTURE OF HUMAN IPS-1 CARD

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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