6ded

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==Crystal structure of the C-terminal ARM domain of Homo sapiens SPIN90 (SH3-protein interacting with Nck), residues 351-722==
==Crystal structure of the C-terminal ARM domain of Homo sapiens SPIN90 (SH3-protein interacting with Nck), residues 351-722==
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<StructureSection load='6ded' size='340' side='right' caption='[[6ded]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='6ded' size='340' side='right'caption='[[6ded]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ded]] is a 2 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=6DED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DED FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ded]] 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=6DED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DED FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.204&#8491;</td></tr>
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<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=6ded FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ded OCA], [http://pdbe.org/6ded PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ded RCSB], [http://www.ebi.ac.uk/pdbsum/6ded PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ded ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ded FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ded OCA], [https://pdbe.org/6ded PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ded RCSB], [https://www.ebi.ac.uk/pdbsum/6ded PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ded ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/SPN90_HUMAN SPN90_HUMAN]] A chromosomal aberration involving NCKIPSD/AF3p21 is found in therapy-related leukemia. Translocation t(3;11)(p21;q23) with KMT2A/MLL1.<ref>PMID:10648423</ref>
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[https://www.uniprot.org/uniprot/SPN90_HUMAN SPN90_HUMAN] A chromosomal aberration involving NCKIPSD/AF3p21 is found in therapy-related leukemia. Translocation t(3;11)(p21;q23) with KMT2A/MLL1.<ref>PMID:10648423</ref>
== Function ==
== Function ==
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[[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>
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[https://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ded" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Luan, Q]]
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[[Category: Large Structures]]
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[[Category: Nolen, B J]]
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[[Category: Luan Q]]
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[[Category: And 2-3 armadillo repeat]]
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[[Category: Nolen BJ]]
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[[Category: Endocytosis]]
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[[Category: Inactive form]]
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[[Category: N-terminally truncated spin90]]
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[[Category: Unable to activate arp2-3 complex]]
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Current revision

Crystal structure of the C-terminal ARM domain of Homo sapiens SPIN90 (SH3-protein interacting with Nck), residues 351-722

PDB ID 6ded

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