3wps

From Proteopedia

(Difference between revisions)

Revision as of 05:45, 3 August 2022

crystal structure of the GAP domain of MgcRacGAP(S387D)

Structural highlights

3wps 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:
NonStd Res:
Related:	3wpq
Gene:	RACGAP1, KIAA1478, MGCRACGAP (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RGAP1_HUMAN] Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11] ^[12]

References

↑ Kawashima T, Hirose K, Satoh T, Kaneko A, Ikeda Y, Kaziro Y, Nosaka T, Kitamura T. MgcRacGAP is involved in the control of growth and differentiation of hematopoietic cells. Blood. 2000 Sep 15;96(6):2116-24. PMID:10979956
↑ Toure A, Dorseuil O, Morin L, Timmons P, Jegou B, Reibel L, Gacon G. MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male germ cells. J Biol Chem. 1998 Mar 13;273(11):6019-23. PMID:9497316
↑ Hirose K, Kawashima T, Iwamoto I, Nosaka T, Kitamura T. MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody. J Biol Chem. 2001 Feb 23;276(8):5821-8. Epub 2000 Nov 20. PMID:11085985 doi:http://dx.doi.org/10.1074/jbc.M007252200
↑ Toure A, Morin L, Pineau C, Becq F, Dorseuil O, Gacon G. Tat1, a novel sulfate transporter specifically expressed in human male germ cells and potentially linked to rhogtpase signaling. J Biol Chem. 2001 Jun 8;276(23):20309-15. Epub 2001 Mar 5. PMID:11278976 doi:http://dx.doi.org/10.1074/jbc.M011740200
↑ Mishima M, Kaitna S, Glotzer M. Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity. Dev Cell. 2002 Jan;2(1):41-54. PMID:11782313
↑ Lee JS, Kamijo K, Ohara N, Kitamura T, Miki T. MgcRacGAP regulates cortical activity through RhoA during cytokinesis. Exp Cell Res. 2004 Feb 15;293(2):275-82. PMID:14729465
↑ Oceguera-Yanez F, Kimura K, Yasuda S, Higashida C, Kitamura T, Hiraoka Y, Haraguchi T, Narumiya S. Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in mitosis. J Cell Biol. 2005 Jan 17;168(2):221-32. Epub 2005 Jan 10. PMID:15642749 doi:10.1083/jcb.200408085
↑ Yuce O, Piekny A, Glotzer M. An ECT2-centralspindlin complex regulates the localization and function of RhoA. J Cell Biol. 2005 Aug 15;170(4):571-82. PMID:16103226 doi:10.1083/jcb.200501097
↑ Zhao WM, Fang G. MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13158-63. Epub 2005 Aug 29. PMID:16129829 doi:http://dx.doi.org/0504145102
↑ Kamijo K, Ohara N, Abe M, Uchimura T, Hosoya H, Lee JS, Miki T. Dissecting the role of Rho-mediated signaling in contractile ring formation. Mol Biol Cell. 2006 Jan;17(1):43-55. Epub 2005 Oct 19. PMID:16236794 doi:10.1091/mbc.E05-06-0569
↑ Burkard ME, Maciejowski J, Rodriguez-Bravo V, Repka M, Lowery DM, Clauser KR, Zhang C, Shokat KM, Carr SA, Yaffe MB, Jallepalli PV. Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells. PLoS Biol. 2009 May 5;7(5):e1000111. doi: 10.1371/journal.pbio.1000111. Epub 2009, May 26. PMID:19468302 doi:10.1371/journal.pbio.1000111
↑ Wolfe BA, Takaki T, Petronczki M, Glotzer M. Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation. PLoS Biol. 2009 May 5;7(5):e1000110. doi: 10.1371/journal.pbio.1000110. Epub 2009, May 26. PMID:19468300 doi:10.1371/journal.pbio.1000110

1 Structural highlights
2 Function
3 See Also
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3wps"

@@ Line 1: / Line 1: @@
 ==crystal structure of the GAP domain of MgcRacGAP(S387D)==
-<StructureSection load='3wps' size='340' side='right' caption='[[3wps]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='3wps' size='340' side='right'caption='[[3wps]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3wps]] 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=3WPS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WPS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3wps]] 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=3WPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WPS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wpq|3wpq]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wpq|3wpq]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RACGAP1, KIAA1478, MGCRACGAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RACGAP1, KIAA1478, MGCRACGAP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3wps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wps OCA], [http://pdbe.org/3wps PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wps RCSB], [http://www.ebi.ac.uk/pdbsum/3wps PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wps 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=3wps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wps OCA], [https://pdbe.org/3wps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wps RCSB], [https://www.ebi.ac.uk/pdbsum/3wps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wps ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RGAP1_HUMAN RGAP1_HUMAN]] Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells.<ref>PMID:10979956</ref> <ref>PMID:9497316</ref> <ref>PMID:11085985</ref> <ref>PMID:11278976</ref> <ref>PMID:11782313</ref> <ref>PMID:14729465</ref> <ref>PMID:15642749</ref> <ref>PMID:16103226</ref> <ref>PMID:16129829</ref> <ref>PMID:16236794</ref> <ref>PMID:19468302</ref> <ref>PMID:19468300</ref>
+[[https://www.uniprot.org/uniprot/RGAP1_HUMAN RGAP1_HUMAN]] Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells.<ref>PMID:10979956</ref> <ref>PMID:9497316</ref> <ref>PMID:11085985</ref> <ref>PMID:11278976</ref> <ref>PMID:11782313</ref> <ref>PMID:14729465</ref> <ref>PMID:15642749</ref> <ref>PMID:16103226</ref> <ref>PMID:16129829</ref> <ref>PMID:16236794</ref> <ref>PMID:19468302</ref> <ref>PMID:19468300</ref>
 ==See Also==
@@ Line 20: / Line 20: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Kato-murayama, M]]
 [[Category: Kitamura, T]]

3wps

From Proteopedia

Revision as of 05:45, 3 August 2022

crystal structure of the GAP domain of MgcRacGAP(S387D)

Structural highlights

Function

See Also

References

Contents

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