3a8q

From Proteopedia

(Difference between revisions)

Revision as of 16:19, 22 December 2021

Low-resolution crystal structure of the Tiam2 PHCCEx domain

Structural highlights

3a8q is a 4 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3a8n, 3a8p
Gene:	Tiam2, Kiaa2016, Stef (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TIAM2_MOUSE] Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates specifically RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane.^[1] ^[2] ^[3] ^[4] ^[5]

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

Tiam1 and Tiam2 (Tiam1/2) are guanine nucleotide-exchange factors that possess the PH-CC-Ex (pleckstrin homology, coiled coil and extra) region that mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. Crystal structures of the PH-CC-Ex regions revealed a single globular domain, PHCCEx domain, comprising a conventional PH subdomain associated with an antiparallel coiled coil of CC subdomain and a novel three-helical globular Ex subdomain. The PH subdomain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. Mutational and binding studies indicated that CC and Ex subdomains form a positively charged surface for protein binding. We identified two unique acidic sequence motifs in Tiam1/2-interacting proteins for binding to PHCCEx domain, Motif-I in CD44 and ephrinB's and the NMDA receptor, and Motif-II in Par3 and JIP2. Our results suggest the molecular basis by which the Tiam1/2 PHCCEx domain facilitates dual binding to membranes and signalling proteins.

The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.,Terawaki S, Kitano K, Mori T, Zhai Y, Higuchi Y, Itoh N, Watanabe T, Kaibuchi K, Hakoshima T EMBO J. 2010 Jan 6;29(1):236-50. Epub 2009 Nov 5. PMID:19893486^[6]

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

References

↑ Hoshino M, Sone M, Fukata M, Kuroda S, Kaibuchi K, Nabeshima Y, Hama C. Identification of the stef gene that encodes a novel guanine nucleotide exchange factor specific for Rac1. J Biol Chem. 1999 Jun 18;274(25):17837-44. PMID:10364228
↑ Matsuo N, Hoshino M, Yoshizawa M, Nabeshima Y. Characterization of STEF, a guanine nucleotide exchange factor for Rac1, required for neurite growth. J Biol Chem. 2002 Jan 25;277(4):2860-8. Epub 2001 Nov 13. PMID:11707441 doi:http://dx.doi.org/10.1074/jbc.M106186200
↑ Kawauchi T, Chihama K, Nabeshima Y, Hoshino M. The in vivo roles of STEF/Tiam1, Rac1 and JNK in cortical neuronal migration. EMBO J. 2003 Aug 15;22(16):4190-201. PMID:12912917 doi:http://dx.doi.org/10.1093/emboj/cdg413
↑ Matsuo N, Terao M, Nabeshima Y, Hoshino M. Roles of STEF/Tiam1, guanine nucleotide exchange factors for Rac1, in regulation of growth cone morphology. Mol Cell Neurosci. 2003 Sep;24(1):69-81. PMID:14550769
↑ Takefuji M, Mori K, Morita Y, Arimura N, Nishimura T, Nakayama M, Hoshino M, Iwamatsu A, Murohara T, Kaibuchi K, Amano M. Rho-kinase modulates the function of STEF, a Rac GEF, through its phosphorylation. Biochem Biophys Res Commun. 2007 Apr 13;355(3):788-94. Epub 2007 Feb 14. PMID:17320046 doi:http://dx.doi.org/10.1016/j.bbrc.2007.02.028
↑ Terawaki S, Kitano K, Mori T, Zhai Y, Higuchi Y, Itoh N, Watanabe T, Kaibuchi K, Hakoshima T. The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module. EMBO J. 2010 Jan 6;29(1):236-50. Epub 2009 Nov 5. PMID:19893486 doi:10.1038/emboj.2009.323

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3a8q"

@@ Line 1: / Line 1: @@
 ==Low-resolution crystal structure of the Tiam2 PHCCEx domain==
-<StructureSection load='3a8q' size='340' side='right' caption='[[3a8q]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<StructureSection load='3a8q' size='340' side='right'caption='[[3a8q]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3a8q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A8Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3a8q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A8Q FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a8n|3a8n]], [[3a8p|3a8p]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a8n|3a8n]], [[3a8p|3a8p]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tiam2, Kiaa2016, Stef ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tiam2, Kiaa2016, Stef ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3a8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8q OCA], [http://pdbe.org/3a8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a8q RCSB], [http://www.ebi.ac.uk/pdbsum/3a8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8q 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=3a8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8q OCA], [https://pdbe.org/3a8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a8q RCSB], [https://www.ebi.ac.uk/pdbsum/3a8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TIAM2_MOUSE TIAM2_MOUSE]] Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates specifically RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane.<ref>PMID:10364228</ref> <ref>PMID:11707441</ref> <ref>PMID:12912917</ref> <ref>PMID:14550769</ref> <ref>PMID:17320046</ref>
+[[https://www.uniprot.org/uniprot/TIAM2_MOUSE TIAM2_MOUSE]] Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates specifically RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane.<ref>PMID:10364228</ref> <ref>PMID:11707441</ref> <ref>PMID:12912917</ref> <ref>PMID:14550769</ref> <ref>PMID:17320046</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Lk3 transgenic mice]]
 [[Category: Hakoshima, T]]

3a8q

From Proteopedia

Revision as of 16:19, 22 December 2021

Low-resolution crystal structure of the Tiam2 PHCCEx domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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