2wmo

From Proteopedia

(Difference between revisions)

Revision as of 11:10, 6 April 2022

Structure of the complex between DOCK9 and Cdc42.

Structural highlights

2wmo is a 2 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:	1wg7, 1am4, 1nf3, 1doa, 1aje, 1ki1, 1gzs, 1kzg, 1cee, 2wmn, 2dfk, 1ees, 1an0, 1kz7, 1e0a, 1a4r, 2wm9, 2ase, 1cf4, 2ngr, 1grn
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DOCK9_HUMAN] Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation.^[1] ^[2]

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

Activation of Rho guanosine triphosphatases (GTPases) to the guanine triphosphate (GTP)-bound state is a critical event in their regulation of the cytoskeleton and cell signaling. Members of the DOCK family of guanine nucleotide exchange factors (GEFs) are important activators of Rho GTPases, but the mechanism of activation by their catalytic DHR2 domain is unknown. Through structural analysis of DOCK9-Cdc42 complexes, we identify a nucleotide sensor within the alpha10 helix of the DHR2 domain that contributes to release of guanine diphosphate (GDP) and then to discharge of the activated GTP-bound Cdc42. Magnesium exclusion, a critical factor in promoting GDP release, is mediated by a conserved valine residue within this sensor, whereas binding of GTP-Mg2+ to the nucleotide-free complex results in magnesium-inducing displacement of the sensor to stimulate discharge of Cdc42-GTP. These studies identify an unusual mechanism of GDP release and define the complete GEF catalytic cycle from GDP dissociation followed by GTP binding and discharge of the activated GTPase.

Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor.,Yang J, Zhang Z, Roe SM, Marshall CJ, Barford D Science. 2009 Sep 11;325(5946):1398-402. PMID:19745154^[3]

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

References

↑ Meller N, Irani-Tehrani M, Kiosses WB, Del Pozo MA, Schwartz MA. Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins. Nat Cell Biol. 2002 Sep;4(9):639-47. PMID:12172552 doi:http://dx.doi.org/10.1038/ncb835
↑ Yang J, Zhang Z, Roe SM, Marshall CJ, Barford D. Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor. Science. 2009 Sep 11;325(5946):1398-402. PMID:19745154 doi:325/5946/1398
↑ Yang J, Zhang Z, Roe SM, Marshall CJ, Barford D. Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor. Science. 2009 Sep 11;325(5946):1398-402. PMID:19745154 doi:325/5946/1398

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='2wmo' size='340' side='right'caption='[[2wmo]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wmo]] is a 2 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=2WMO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WMO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wmo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WMO FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wg7|1wg7]], [[1am4|1am4]], [[1nf3|1nf3]], [[1doa|1doa]], [[1aje|1aje]], [[1ki1|1ki1]], [[1gzs|1gzs]], [[1kzg|1kzg]], [[1cee|1cee]], [[2wmn|2wmn]], [[2dfk|2dfk]], [[1ees|1ees]], [[1an0|1an0]], [[1kz7|1kz7]], [[1e0a|1e0a]], [[1a4r|1a4r]], [[2wm9|2wm9]], [[2ase|2ase]], [[1cf4|1cf4]], [[2ngr|2ngr]], [[1grn|1grn]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wg7|1wg7]], [[1am4|1am4]], [[1nf3|1nf3]], [[1doa|1doa]], [[1aje|1aje]], [[1ki1|1ki1]], [[1gzs|1gzs]], [[1kzg|1kzg]], [[1cee|1cee]], [[2wmn|2wmn]], [[2dfk|2dfk]], [[1ees|1ees]], [[1an0|1an0]], [[1kz7|1kz7]], [[1e0a|1e0a]], [[1a4r|1a4r]], [[2wm9|2wm9]], [[2ase|2ase]], [[1cf4|1cf4]], [[2ngr|2ngr]], [[1grn|1grn]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wmo OCA], [http://pdbe.org/2wmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wmo RCSB], [http://www.ebi.ac.uk/pdbsum/2wmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wmo 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=2wmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wmo OCA], [https://pdbe.org/2wmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wmo RCSB], [https://www.ebi.ac.uk/pdbsum/2wmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wmo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DOCK9_HUMAN DOCK9_HUMAN]] Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation.<ref>PMID:12172552</ref> <ref>PMID:19745154</ref>
+[[https://www.uniprot.org/uniprot/DOCK9_HUMAN DOCK9_HUMAN]] Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP. Overexpression induces filopodia formation.<ref>PMID:12172552</ref> <ref>PMID:19745154</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2wmo

From Proteopedia

Revision as of 11:10, 6 April 2022

Structure of the complex between DOCK9 and Cdc42.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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