1gil: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1gil.png|left|200px]]


<!--
==STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS==
The line below this paragraph, containing "STRUCTURE_1gil", creates the "Structure Box" on the page.
<StructureSection load='1gil' size='340' side='right'caption='[[1gil]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1gil]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GIL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GIL FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1gil|  PDB=1gil  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gil FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gil OCA], [https://pdbe.org/1gil PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gil RCSB], [https://www.ebi.ac.uk/pdbsum/1gil PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gil ProSAT]</span></td></tr>
 
</table>
===STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS===
== Function ==
 
[https://www.uniprot.org/uniprot/GNAI1_RAT GNAI1_RAT] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:16870394</ref>
 
== Evolutionary Conservation ==
<!--
[[Image:Consurf_key_small.gif|200px|right]]
The line below this paragraph, {{ABSTRACT_PUBMED_8073283}}, adds the Publication Abstract to the page
Check<jmol>
(as it appears on PubMed at http://www.pubmed.gov), where 8073283 is the PubMed ID number.
  <jmolCheckbox>
-->
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gi/1gil_consurf.spt"</scriptWhenChecked>
{{ABSTRACT_PUBMED_8073283}}
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1GIL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GIL OCA].  
</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=1gil ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis., Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR, Science. 1994 Sep 2;265(5177):1405-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8073283 8073283]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Berghuis AM]]
[[Category: Berghuis, A M.]]
[[Category: Coleman DE]]
[[Category: Coleman, D E.]]
[[Category: Sprang SR]]
[[Category: Sprang, S R.]]
[[Category: Gtp-binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 05:21:05 2008''

Latest revision as of 10:25, 7 February 2024

STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSISSTRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS

Structural highlights

1gil is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GNAI1_RAT Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.[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. Shu FJ, Ramineni S, Amyot W, Hepler JR. Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization. Cell Signal. 2007 Jan;19(1):163-76. Epub 2006 Jul 25. PMID:16870394 doi:http://dx.doi.org/10.1016/j.cellsig.2006.06.002

1gil, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA