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| | ==Crystal Structure of Human DAAM1 FH2== | | ==Crystal Structure of Human DAAM1 FH2== |
| - | <StructureSection load='2z6e' size='340' side='right' caption='[[2z6e]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='2z6e' size='340' side='right'caption='[[2z6e]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2z6e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z6E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2z6e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z6E FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ux5|1ux5]], [[1y64|1y64]], [[1v9d|1v9d]]</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;'>[[1ux5|1ux5]], [[1y64|1y64]], [[1v9d|1v9d]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAAM1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2z6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z6e OCA], [http://pdbe.org/2z6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z6e RCSB], [http://www.ebi.ac.uk/pdbsum/2z6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2z6e 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=2z6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z6e OCA], [https://pdbe.org/2z6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z6e RCSB], [https://www.ebi.ac.uk/pdbsum/2z6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z6e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DAAM1_HUMAN DAAM1_HUMAN]] Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments.<ref>PMID:16630611</ref> <ref>PMID:17482208</ref> | + | [[https://www.uniprot.org/uniprot/DAAM1_HUMAN DAAM1_HUMAN]] Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments.<ref>PMID:16630611</ref> <ref>PMID:17482208</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Fukai, S]] | | [[Category: Fukai, S]] |
| | [[Category: Higashi, T]] | | [[Category: Higashi, T]] |
| Structural highlights
Function
[DAAM1_HUMAN] Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments.[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
Reorganization of the actin filament is an essential process for cell motility, cell-cell attachment and intracellular transport. Formin proteins promote nucleation and elongation of the actin filament, and thus are key regulators for this process. The formin homology 2 (FH2) domain forms a head-to-tail ring-shaped dimer, and processively moves towards the barbed end. Dishevelled-associated activator of morphogenesis (DAAM) is a Rho-regulated formin implicated in neuronal development. Here, we present the crystal structure of human DAAM1 FH2 dimer at 2.8 A resolution. This is the first dimeric structure of the mammalian formin. The core structure of human DAAM1 is similar to those of mouse mDia1 and yeast Bni1p, whereas the orientations of the FH2 dimeric rings are different between human DAAM1 and yeast Bni1p, despite their similar dimer interactions. This difference supports the previous prediction that the dimer architecture of the formin is highly flexible in the actin-free state. The results of the actin assembly assays using the DAAM1 mutants demonstrated that the length of the linker connecting the N-terminal domain and the core region is crucial for the activity.
Crystal structure of human DAAM1 formin homology 2 domain.,Yamashita M, Higashi T, Suetsugu S, Sato Y, Ikeda T, Shirakawa R, Kita T, Takenawa T, Horiuchi H, Fukai S, Nureki O Genes Cells. 2007 Nov;12(11):1255-65. PMID:17986009[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aspenstrom P, Richnau N, Johansson AS. The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics. Exp Cell Res. 2006 Jul 15;312(12):2180-94. Epub 2006 Apr 21. PMID:16630611 doi:http://dx.doi.org/10.1016/j.yexcr.2006.03.013
- ↑ Lu J, Meng W, Poy F, Maiti S, Goode BL, Eck MJ. Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly. J Mol Biol. 2007 Jun 22;369(5):1258-69. Epub 2007 Apr 5. PMID:17482208 doi:10.1016/j.jmb.2007.04.002
- ↑ Yamashita M, Higashi T, Suetsugu S, Sato Y, Ikeda T, Shirakawa R, Kita T, Takenawa T, Horiuchi H, Fukai S, Nureki O. Crystal structure of human DAAM1 formin homology 2 domain. Genes Cells. 2007 Nov;12(11):1255-65. PMID:17986009 doi:10.1111/j.1365-2443.2007.01132.x
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