3dad
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='3dad' size='340' side='right'caption='[[3dad]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3dad' size='340' side='right'caption='[[3dad]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3dad]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3dad]] is a 2 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=3DAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DAD FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=3dad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dad OCA], [https://pdbe.org/3dad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dad RCSB], [https://www.ebi.ac.uk/pdbsum/3dad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dad 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=3dad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dad OCA], [https://pdbe.org/3dad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dad RCSB], [https://www.ebi.ac.uk/pdbsum/3dad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dad ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/FHOD1_HUMAN FHOD1_HUMAN] Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing.<ref>PMID:14576350</ref> <ref>PMID:15878344</ref> <ref>PMID:18694941</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 19: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dad ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dad ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Formins induce the nucleation and polymerization of unbranched actin filaments. They share three homology domains required for profilin binding, actin polymerization, and regulation. Diaphanous-related formins (DRFs) are activated by GTPases of the Rho/Rac family, whose interaction with the N-terminal formin domain is thought to displace a C-terminal Diaphanous-autoregulatory domain (DAD). We have determined the structure of the N-terminal domains of FHOD1 consisting of a GTPase-binding domain (GBD) and the DAD-recognition domain FH3. In contrast to the formin mDia1, the FHOD1-GBD reveals a ubiquitin superfold as found similarly in c-Raf1 or PI3 kinase. This GBD is recruited by Rac and Ras GTPases in cells and plays an essential role for FHOD1-mediated actin remodeling. The FHOD1-FH3 domain is composed of five armadillo repeats, similarly to other formins. Mutation of one residue in the predicted DAD-interaction surface efficiently activates FHOD1 in cells. These results demonstrate that DRFs have evolved different molecular solutions to govern their autoregulation and GTPase specificity. | ||
| - | |||
| - | The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation.,Schulte A, Stolp B, Schonichen A, Pylypenko O, Rak A, Fackler OT, Geyer M Structure. 2008 Sep 10;16(9):1313-23. PMID:18786395<ref>PMID:18786395</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3dad" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Fackler | + | [[Category: Fackler OT]] |
| - | [[Category: Geyer | + | [[Category: Geyer M]] |
| - | [[Category: Pylypenko | + | [[Category: Pylypenko O]] |
| - | [[Category: Rak | + | [[Category: Rak A]] |
| - | [[Category: Schonichen | + | [[Category: Schonichen A]] |
| - | [[Category: Schulte | + | [[Category: Schulte A]] |
| - | [[Category: Stolp | + | [[Category: Stolp B]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the N-terminal regulatory domains of the formin FHOD1
| |||||||||||
Categories: Homo sapiens | Large Structures | Fackler OT | Geyer M | Pylypenko O | Rak A | Schonichen A | Schulte A | Stolp B
