1x1f: Difference between revisions

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==Solution structure of the PH domain of human Docking protein BRDG1==
==Solution structure of the PH domain of human Docking protein BRDG1==
<StructureSection load='1x1f' size='340' side='right' caption='[[1x1f]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1x1f' size='340' side='right'caption='[[1x1f]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1x1f]] 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=1X1F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X1F FirstGlance]. <br>
<table><tr><td colspan='2'>[[1x1f]] 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=1X1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X1F FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">brdg1 ([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=1x1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x1f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1x1f RCSB], [http://www.ebi.ac.uk/pdbsum/1x1f PDBsum], [http://www.topsan.org/Proteins/RSGI/1x1f 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=1x1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x1f OCA], [https://pdbe.org/1x1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x1f RCSB], [https://www.ebi.ac.uk/pdbsum/1x1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x1f ProSAT], [https://www.topsan.org/Proteins/RSGI/1x1f TOPSAN]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/STAP1_HUMAN STAP1_HUMAN] In BCR signaling, appears to function as a docking protein acting downstream of TEC and participates in a positive feedback loop by increasing the activity of TEC.<ref>PMID:10518561</ref>  
== 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/x1/1x1f_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x1/1x1f_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=1x1f ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__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: Docking protein brdg1]]
[[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 16:55, 9 May 2024

Solution structure of the PH domain of human Docking protein BRDG1Solution structure of the PH domain of human Docking protein BRDG1

Structural highlights

1x1f 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

STAP1_HUMAN In BCR signaling, appears to function as a docking protein acting downstream of TEC and participates in a positive feedback loop by increasing the activity of TEC.[1]

Evolutionary Conservation

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

References

  1. Ohya K, Kajigaya S, Kitanaka A, Yoshida K, Miyazato A, Yamashita Y, Yamanaka T, Ikeda U, Shimada K, Ozawa K, Mano H. Molecular cloning of a docking protein, BRDG1, that acts downstream of the Tec tyrosine kinase. Proc Natl Acad Sci U S A. 1999 Oct 12;96(21):11976-81. PMID:10518561
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