7y4n
From Proteopedia
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<StructureSection load='7y4n' size='340' side='right'caption='[[7y4n]]' scene=''> | <StructureSection load='7y4n' size='340' side='right'caption='[[7y4n]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[7y4n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y4N FirstGlance]. <br> |
</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=7y4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y4n OCA], [https://pdbe.org/7y4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y4n RCSB], [https://www.ebi.ac.uk/pdbsum/7y4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y4n ProSAT]</span></td></tr> | </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=7y4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y4n OCA], [https://pdbe.org/7y4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y4n RCSB], [https://www.ebi.ac.uk/pdbsum/7y4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y4n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/GRAP_DROME GRAP_DROME]] Adapter protein which modulates signaling mediated by several receptor tyrosine kinases such as sev and Ack (PubMed:8462097, PubMed:22615583, PubMed:8462098). Required for proper signaling by sevenless (PubMed:8462097, PubMed:8462098). May act to stimulate the ability of Sos to catalyze Ras1 activation by linking sevenless and Sos in a signaling complex (PubMed:8462097, PubMed:8462098). Required for functional and morphological integrities of the scolopidia, sensory neurons and the antennal mechanosensory and motor center (AMMC) brain neuropil (PubMed:30610177). Required for Ack-dependent suppression of apoptosis in the eye (PubMed:22615583).<ref>PMID:22615583</ref> <ref>PMID:30610177</ref> <ref>PMID:8462097</ref> <ref>PMID:8462098</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Drk, a Drosophila homologue of human GRB2, interacts with Sevenless (Sev) receptor via its SH2 domain, while the N- and C-terminal SH3 domains (Drk-NSH3 and Drk-CSH3, respectively) are responsible for the interaction with proline-rich motifs (PRMs) of Son of sevenless (Sos) or Daughter of Sevenless (Dos). Drk-NSH3 on its own has a conformational equilibrium between folded and unfolded states, and the folded state is stabilised by the association with a Sos-derived proline-rich peptide with PxxPxR motif. In contrast, Drk-CSH3 is supposed to bind PxxxRxxKP motifs in Dos. Aiming at clarifying the structural and functional differences between the two SH3 domains, we performed NMR studies of Drk-CSH3. The resulting solution structure and the (15)N-relaxation data showed that Drk-CSH3 consists of a stable domain. Large chemical shift perturbation was commonly found around the RT loop and the hydrophobic patch, while there were also changes that occur characteristically for Sos- or Dos-derived peptides. Sos-derived two peptides with PxxPxR motif showed stronger affinity to Drk-CSH3, indicating that the Sos PRMs can bind both N- and C-SH3 domains. Dos-derived two peptides could also bind Drk-CSH3, but with much weaker affinity, suggesting a possibility that any cooperative binding of Dos-PRMs may strengthen the Drk-Dos interaction. The NMR studies as well as the docking simulations provide valuable insights into the biological and biophysical functions of two SH3 domains in Drk. | ||
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| + | Insight into the C-terminal SH3 domain mediated binding of Drosophila Drk to Sos and Dos.,Sayeesh PM, Ikeya T, Sugasawa H, Watanabe R, Mishima M, Inomata K, Ito Y Biochem Biophys Res Commun. 2022 Oct 15;625:87-93. doi:, 10.1016/j.bbrc.2022.08.007. Epub 2022 Aug 5. PMID:35952612<ref>PMID:35952612</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7y4n" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ikeya T]] | [[Category: Ikeya T]] | ||
Current revision
Insight into the C-terminal SH3 domain mediated binding of Drosophila Drk to Sos and Dos
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