3thf: Difference between revisions
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==Crystal structure of the SD2 domain from Drosophila Shroom== | ==Crystal structure of the SD2 domain from Drosophila Shroom== | ||
<StructureSection load='3thf' size='340' side='right' caption='[[3thf]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3thf' size='340' side='right'caption='[[3thf]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3thf]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3thf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3THF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3THF FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG34379, Shroom ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG34379, Shroom ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3thf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3thf OCA], [https://pdbe.org/3thf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3thf RCSB], [https://www.ebi.ac.uk/pdbsum/3thf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3thf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SHRM_DROME SHRM_DROME]] May be involved in the assembly of microtubule arrays during cell elongation (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Drome]] | [[Category: Drome]] | ||
[[Category: Large Structures]] | |||
[[Category: Mohan, S]] | [[Category: Mohan, S]] | ||
[[Category: VanDemark, A P]] | [[Category: VanDemark, A P]] | ||
Revision as of 19:58, 6 July 2022
Crystal structure of the SD2 domain from Drosophila ShroomCrystal structure of the SD2 domain from Drosophila Shroom
Structural highlights
Function[SHRM_DROME] May be involved in the assembly of microtubule arrays during cell elongation (By similarity). Publication Abstract from PubMedShroom (Shrm) proteins are essential regulators of cell shape and tissue morpho-logy during animal development that function by interacting directly with the coiled-coil region of Rho kinase (Rock). The Shrm-Rock interaction is sufficient to direct Rock subcellular localization and the subsequent assembly of contractile actomyosin networks in defined subcellular locales. However, it is unclear how the Shrm-Rock interaction is regulated at the molecular level. To begin investigating this issue, we present the structure of Shrm domain 2 (SD2), which mediates the interaction with Rock and is required for Shrm function. SD2 is a unique three-segmented dimer with internal symmetry, and we identify conserved residues on the surface and within the dimerization interface that are required for the Rock-Shrm interaction and Shrm activity in vivo. We further show that these residues are critical in both vertebrate and invertebrate Shroom proteins, indicating that the Shrm-Rock signaling module has been functionally and molecularly conserved. The structure and biochemical analysis of Shrm SD2 indicate that it is distinct from other Rock activators such as RhoA and establishes a new paradigm for the Rock-mediated assembly of contractile actomyosin networks. Structure of Shroom domain 2 reveals a three-segmented coiled-coil required for dimerization, Rock binding, and apical constriction.,Mohan S, Rizaldy R, Das D, Bauer RJ, Heroux A, Trakselis MA, Hildebrand JD, Vandemark AP Mol Biol Cell. 2012 Jun;23(11):2131-42. Epub 2012 Apr 4. PMID:22493320[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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