6dee
From Proteopedia
(Difference between revisions)
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<StructureSection load='6dee' size='340' side='right' caption='[[6dee]], [[Resolution|resolution]] 3.04Å' scene=''> | <StructureSection load='6dee' size='340' side='right' caption='[[6dee]], [[Resolution|resolution]] 3.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6dee]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DEE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dee]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DEE FirstGlance]. <br> |
| - | </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=6dee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dee OCA], [http://pdbe.org/6dee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dee RCSB], [http://www.ebi.ac.uk/pdbsum/6dee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dee ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NCKIPSD, AF3P21, SPIN90 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6dee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dee OCA], [http://pdbe.org/6dee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dee RCSB], [http://www.ebi.ac.uk/pdbsum/6dee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dee ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SPN90_HUMAN SPN90_HUMAN]] Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1). Induces microspike formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42 (By similarity). May play an important role in the maintenance of sarcomeres and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. Plays a role in angiogenesis.<ref>PMID:22419821</ref> | [[http://www.uniprot.org/uniprot/SPN90_HUMAN SPN90_HUMAN]] Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1). Induces microspike formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42 (By similarity). May play an important role in the maintenance of sarcomeres and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. Plays a role in angiogenesis.<ref>PMID:22419821</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Unlike the WASP family of Arp2/3 complex activators, WISH/DIP/SPIN90 (WDS) family proteins activate actin filament nucleation by the Arp2/3 complex without the need for a preformed actin filament. This allows WDS proteins to initiate branched actin network assembly by providing seed filaments that activate WASP-bound Arp2/3 complex. Despite their important role in actin network initiation, it is unclear how WDS proteins drive the activating steps that require both WASP and pre-existing actin filaments during WASP-mediated nucleation. Here, we show that SPIN90 folds into an armadillo repeat domain that binds a surface of Arp2/3 complex distinct from the two WASP sites, straddling a hinge point that may stimulate movement of the Arp2 subunit into the activated short-pitch conformation. SPIN90 binds a surface on Arp2/3 complex that overlaps with actin filament binding, explaining how it could stimulate the same structural rearrangements in the complex as pre-existing actin filaments. By revealing how WDS proteins activate the Arp2/3 complex, these data provide a molecular foundation to understand initiation of dendritic actin networks and regulation of Arp2/3 complex by its activators. | ||
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| + | Structure of the nucleation-promoting factor SPIN90 bound to the actin filament nucleator Arp2/3 complex.,Luan Q, Liu SL, Helgeson LA, Nolen BJ EMBO J. 2018 Oct 15. pii: embj.2018100005. doi: 10.15252/embj.2018100005. PMID:30322896<ref>PMID:30322896</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6dee" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Luan, Q]] | [[Category: Luan, Q]] | ||
[[Category: Nolen, B J]] | [[Category: Nolen, B J]] | ||
Revision as of 07:14, 31 October 2018
Crystal structure of the C-terminus of Homo sapiens SPIN90 (SH3-protein interacting with Nck), residues 306-722
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