2cod: Difference between revisions

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==Solution structure of the N-terminal PH domain of ARAP2 protein from human==
==Solution structure of the N-terminal PH domain of ARAP2 protein from human==
<StructureSection load='2cod' size='340' side='right' caption='[[2cod]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2cod' size='340' side='right'caption='[[2cod]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2COD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2COD FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cod]] is a 1 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=2COD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2COD FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARAP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cod RCSB], [http://www.ebi.ac.uk/pdbsum/2cod PDBsum], [http://www.topsan.org/Proteins/RSGI/2cod TOPSAN]</span></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=2cod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cod OCA], [https://pdbe.org/2cod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cod RCSB], [https://www.ebi.ac.uk/pdbsum/2cod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cod ProSAT], [https://www.topsan.org/Proteins/RSGI/2cod TOPSAN]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARAP2_HUMAN ARAP2_HUMAN] Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/2cod_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/2cod_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=2cod ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Inoue, M.]]
[[Category: Large Structures]]
[[Category: Kigawa, T.]]
[[Category: Inoue M]]
[[Category: Koshiba, S.]]
[[Category: Kigawa T]]
[[Category: Li, H.]]
[[Category: Koshiba S]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Li H]]
[[Category: Tomizawa, T.]]
[[Category: Tomizawa T]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama S]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Ph domain]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Signaling protein]]
[[Category: Structural genomic]]

Latest revision as of 14:27, 22 May 2024

Solution structure of the N-terminal PH domain of ARAP2 protein from humanSolution structure of the N-terminal PH domain of ARAP2 protein from human

Structural highlights

2cod is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

ARAP2_HUMAN Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency (By similarity).

Evolutionary Conservation

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

Drag the structure with the mouse to rotate

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