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5kdo

From Proteopedia

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Heterotrimeric complex of the 4 alanine insertion variant of the Gi alpha1 subunit and the Gbeta1-Ggamma1

Structural highlights

5kdo is a 3 chain structure with sequence from Bos taurus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
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]

Publication Abstract from PubMed

G protein coupled receptor (GPCR) mediated heterotrimeric G protein activation is a major mode of signal transduction in the cell. Previously, we and other groups reported that the alpha 5 (alpha5) helix of Galphai1, especially the hydrophobic interactions in this region, plays a key role during nucleotide release and G protein activation. To further investigate the effect of this hydrophobic core, we disrupted it in Galphai1 by inserting 4 alanine amino acids into the alpha5 helix between residues Q333 and F334 (Ins4A). This extends the length of the alpha5 helix without disturbing the beta6-alpha5 loop interactions. This mutant has high basal nucleotide exchange activity, yet no receptor-mediated activation of nucleotide exchange. By using structural approaches, we show that this mutant loses critical hydrophobic interactions leading to significant rearrangements of side chain residues H57, F189, F191, and F336; it also disturbs the rotation of the alpha5 helix, and the pi-pi interaction between H57 and F189. In addition, the insertion mutant abolishes G protein release from the activated receptor after nucleotide binding. Our biochemical and computational data indicate that the interactions between alpha5, alpha1 and beta2-beta3 are not only vital for GDP release during G protein activation, but they are also necessary for proper GTP binding (or GDP re-binding). Thus, our studies suggest that this hydrophobic interface is critical for accurate rearrangement of the alpha5 helix for G protein release from the receptor after GTP binding.

A conserved hydrophobic core in Galphai1 regulates G protein activation and release from activated receptor.,Kaya AI, Lokits AD, Gilbert JA, Iverson TM, Meiler J, Hamm HE J Biol Chem. 2016 Jul 26. pii: jbc.M116.745513. PMID:27462082^[2]

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

References

↑ 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
↑ Kaya AI, Lokits AD, Gilbert JA, Iverson TM, Meiler J, Hamm HE. A conserved hydrophobic core in Galphai1 regulates G protein activation and release from activated receptor. J Biol Chem. 2016 Jul 26. pii: jbc.M116.745513. PMID:27462082 doi:http://dx.doi.org/10.1074/jbc.M116.745513

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5kdo"

@@ Line 1: / Line 1: @@
 ==Heterotrimeric complex of the 4 alanine insertion variant of the Gi alpha1 subunit and the Gbeta1-Ggamma1==
-<StructureSection load='5kdo' size='340' side='right' caption='[[5kdo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='5kdo' size='340' side='right'caption='[[5kdo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5kdo]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KDO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5kdo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KDO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kdl|5kdl]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></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=5kdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kdo OCA], [http://pdbe.org/5kdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kdo RCSB], [http://www.ebi.ac.uk/pdbsum/5kdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kdo ProSAT]</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=5kdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kdo OCA], [https://pdbe.org/5kdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kdo RCSB], [https://www.ebi.ac.uk/pdbsum/5kdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kdo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/GBG1_BOVIN GBG1_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. [[http://www.uniprot.org/uniprot/GBB1_BOVIN GBB1_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5kdo" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transducin 3D structures|Transducin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Gilbert, J]]
+[[Category: Bos taurus]]
-[[Category: Hamm, H E]]
+[[Category: Large Structures]]
-[[Category: Iverson, T M]]
+[[Category: Rattus norvegicus]]
-[[Category: Kaya, A I]]
+[[Category: Gilbert J]]
-[[Category: Lokits, A D]]
+[[Category: Hamm HE]]
-[[Category: Meiler, J]]
+[[Category: Iverson TM]]
-[[Category: Heterotrimeric g protein g protein coupled receptors g protein activation g protein structure gdp release]]
+[[Category: Kaya AI]]
-[[Category: Signaling protein]]
+[[Category: Lokits AD]]
+[[Category: Meiler J]]

5kdo

From Proteopedia

Current revision

Heterotrimeric complex of the 4 alanine insertion variant of the Gi alpha1 subunit and the Gbeta1-Ggamma1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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