3w6r
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of the GAP domain of human MgcRacGAP== | |
| - | + | <StructureSection load='3w6r' size='340' side='right' caption='[[3w6r]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3w6r]] is a 1 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=3W6R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W6R FirstGlance]. <br> | |
| - | ==Function== | + | </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='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=3w6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w6r RCSB], [http://www.ebi.ac.uk/pdbsum/3w6r PDBsum]</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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cytokinesis in animal cells relies on a centralspindlin complex consisting of male germ cell RacGap (MgcRacGAP) and mitotic kinesin-like protein 1 (MKLP1). Rho GTPases act as molecular switches to regulate the actin cytoskeleton for cytokinesis, of which Rac1 is regulated by MgcRacGAP. In this study, we determined the crystal structure of the GTPase-activating protein (GAP) domain of MgcRacGAP at a resolution of 1.9A. The conformation of Arg385, which is a key residue for GAP activity, was found to be different from that of previously reported GAP proteins, and MgcRacGAP (residues 348-546) was found to exist as a monomer in solution, according to Stokes radii. We also measured the GAP activity of MgcRacGAP mutants for Rac1. | ||
| - | + | Crystal structure of GTPase-activating domain from human MgcRacGAP.,Matsuura A, Lee HH Biochem Biophys Res Commun. 2013 Jun 7;435(3):367-72. doi:, 10.1016/j.bbrc.2013.04.094. Epub 2013 May 7. PMID:23665020<ref>PMID:23665020</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Lee, H H | + | == References == |
| - | [[Category: Matsuura, A | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Lee, H H]] | ||
| + | [[Category: Matsuura, A]] | ||
[[Category: Gtpase activating]] | [[Category: Gtpase activating]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 05:19, 25 December 2014
Crystal structure of the GAP domain of human MgcRacGAP
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