3dad
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3dad is ON HOLD Authors: Schulte, A., Stolp, B., Schonichen, A., Pylypenko, O., Rak, A., Fackler, O.T., Geyer, M. Description: Crystal structure of...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the N-terminal regulatory domains of the formin FHOD1== | |
| - | + | <StructureSection load='3dad' size='340' side='right'caption='[[3dad]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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='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> | |
| - | + | </table> | |
| - | + | == 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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/da/3dad_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fackler OT]] | ||
| + | [[Category: Geyer M]] | ||
| + | [[Category: Pylypenko O]] | ||
| + | [[Category: Rak A]] | ||
| + | [[Category: Schonichen A]] | ||
| + | [[Category: Schulte A]] | ||
| + | [[Category: Stolp B]] | ||
Current revision
Crystal structure of the N-terminal regulatory domains of the formin FHOD1
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Categories: Homo sapiens | Large Structures | Fackler OT | Geyer M | Pylypenko O | Rak A | Schonichen A | Schulte A | Stolp B
